ISSN 0006-2979, Biochemistry (Moscow), 2025, Vol. 90, No. 12, pp. 1911-1918 © Pleiades Publishing, Ltd., 2025.
Russian Text © The Author(s), 2025, published in Biokhimiya, 2025, Vol. 90, No. 12, pp. 2012-2020.
1911
REVIEW
From Cellular Architecture to Regulation
of Mitochondrial Function: Role of Vimentin
in Ensuring Cellular Mitostasis
Roaa Deeb
1,2
, Anton S. Shakhov
1,3
, Aleksandra S. Churkina
1,3
, Irina B. Alieva
1,3
,
and Alexander A. Minin
1,a
*
1
Institute of Protein Research, Russian Academy of Sciences,
119334 Moscow, Russia
2
Moscow Institute of Physics and Technology (MIPT),
141701 Dolgoprudny, Moscow Region, Russia
3
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University,
119992 Moscow, Russia
a
e-mail: alexminin@gmail.com
Received August 31, 2025
Revised October 17, 2025
Accepted November 11, 2025
Abstract— Mitochondria play a central role in cell physiology, and in addition to performing their primary
function as an energy source, they are involved in processes such as regulating intracellular calcium levels,
generating reactive oxygen species, synthesizing many critical compounds, regulating apoptosis, and more.
In this regard, maintaining them in a normal state is of great importance, ensuring their transport, intra-
cellular distribution, timely biogenesis, and removal of damaged mitochondria from the cells. All of this
is defined as cellular mitostasis, maintenance of which involves many cellular structures and, primarily,
the cytoskeleton. This review summarizes the data on the role of one component of cytoskeleton, vimentin
intermediate filaments, in these processes.
DOI: 10.1134/S0006297925602813
Keywords: cytoskeleton, microtubules, actin filaments, intermediate filaments, vimentin filaments, mitochondria
* To whom correspondence should be addressed.
INTRODUCTION. MITOCHONDRIA
ARE POWERHOUSES IN CELLS
BUT NOT JUST THAT
Classic notions on mitochondria as organelles
responsible for supplying energy for the cell needs
have been extended significantly in the recent half
century. It was demonstrated in numerous studies
that in addition to supplying energy, mitochondria
also participate in a number of intracellular process-
es not directly associated with oxidation of organic
compounds and generation of energy in form of ATP
molecules (Fig. 1). Mitochondria are among the main
intracellular depots of calcium ions [1], they play an
important role in metabolism regulation, participate
in synthesis of steroid hormones [2] and other com-
pounds, and in regulation of apoptosis [3].
To effectively perform their functions, mitochon-
dria require certain balance of intracellular factors en-
suring, among other things, their correct mitostasis –
maintenance and regulation of the distributed pool
of healthy mitochondria during the entire lifespan of
the cell [4]. The term ‘mitostasis’ is usually under-
stood as combination of such processes as mitochon-
drial respiration, their fusion and fission (depending
on the cell needs), mitochondrial transport, and mi-
tochondria anchoring at the locations of their active
functioning [5]. Furthermore, maintenance of mito-
chondria population in a healthy state is impossible
without removal of damaged proteins and organelles.
DEEB et al.1912
BIOCHEMISTRY (Moscow) Vol. 90 No. 12 2025
Fig. 1. Functions of mitochondria in cells and their effects on different processes. The best-known classical functions of
mitochondria (shown in blue color) are primarily associated with ATP synthesis and oxidation of organic compounds.
However, direct participation of mitochondria in numerous other processes (shown in green color) has been demonstrated
in recent years. Among those: synthesis of steroid hormones, regulation of apoptosis and cell stress, serving as an intra-
cellular depot of calcium ions. Reactive oxygen species (ROS) generated in mitochondria participate in regulation of cell
migration and, at the same time, negatively affect various cellular structures both inside mitochondria and outside of them;
in particular, they could cause damage in various proteins and lipids, as well as they could induce cell aging. Many stud-
ies have been devoted to investigation of factors preventing negative effects of ROS; among those antioxidants have been
investigated in most detail. Moreover, it is known that biogenesis of mitochondria and maintenance of normal mitostasis
also facilitate slowdown of aging.
This process includes degradation of individual mito-
chondrial proteins and whole mitochondria via mito-
phagy and macroautophagy [6].
Quality and number of mitochondria decrease
with aging, which results in the enhanced produc-
tion of ROS that facilitate cell aging [7, 8]. Under
conditions of enhanced production of ROS, oxidative
reactions are induced, which damage nucleic acids,
proteins, and membrane lipids. This, in turn, disrupts
mitochondria functioning and subcellular localization
of different important components, thus causing cel-
lular pathologies [9, 10]. Intracellular levels of ROS
are controlled by a number of enzymes with antiox-
idant activity. The available experimental data indi-
cate a close relationship between the mitochondria
biogenesis and antioxidant activity [11].
That is why the cellular components capable of
mitostasis maintenance or of its normalization in the
case of disruption under the effect of negative factors
attract particular interest of the researchers. One of
the probable candidates for this role is the cell cy-
toskeleton consisting of three fibrillar components –
microtubules, actin microfilaments, and intermediate
filaments (IF). We believe that IFs (vimentin fila-
ments, in particular) are the most likely candidates
for this role, and in this review, we intend to justify
this idea.
CELL CYTOSKELETON AS A PLATFORM
FOR DISTRIBUTION AND MODULATION
OF CELULAR ORGANELLES
Cytoskeleton is a network of microtubules, actin
filaments, and IF, it plays both the role of a rather
rigid carcass of the cell, and the role of dynamic reg-
ulator of the cell organization. This comprehensive
network of protein filaments exhibits a remarkable
ability for rearrangement in response to various in-
ternal and external signals, which facilitates imme-
diate adaptation of the cells to the changing condi-
tions. Cytoskeleton is a key player in many processes
including cell division, cell motility, maintenance of
the cell shape, intracellular transport, and distribu-
tion of different organelles. Interactions of the cyto-
skeleton structures with mitochondria, which mediate
their transport and distribution are of particular in-
terest [12].
While the microtubules mediate long-distance
transport of mitochondria, actin filaments facilitate
their local transport [13]. The transport is realized
with the help of motor proteins, kinesins and dyneins,
in the case of microtubules, and with the help of my-
osins in the case of actin filaments [14]. Direction of
transport along microtubules is determined by their
polarity, as well as by the features of motor proteins,
MITOSTASIS – FOCUS ON VIMENTIN FILAMENTS 1913
BIOCHEMISTRY (Moscow) Vol. 90 No. 12 2025
which move along them only in one direction: almost
all kinesins – towards the so-called plus-end, and
dyneins – towards the minus end. The actin-depen-
dent transport is realized via the action of myosin
motor proteins, which also differ in the direction of
walk along microfilaments. In particular, the myo-
sin V transports cargo towards the fast growing plus
ends of microfilaments, while the myosin VI mediates
transport towards the minus ends [15]. Furthermore,
movement of some organelles could occur as a result
of forces generated by the polymerizing actin [16].
This complex transport system ensures timely deliv-
ery of mitochondria and other organelles to various,
sometimes rather distant parts of the cell. In addition
to transport, the cytoskeleton structures play roles in
maintaining position of the delivered organelles in
the location of their functioning.
Videomicroscopy analysis (time-lapse microsco-
py) of the mitochondria behavior in the fibroblasts
revealed that majority of these organelles are in
the stationary state, and only minor fractions are in
the process of transport along microtubules [17-21].
It was found that motility of mitochondria is under
regulatory control. In particular, one of the growth
factors, lysophosphatidic acid, acting through the
small GTPase RhoA and mDia1 protein associated
with it, inhibits mitochondria movement and causes
their anchoring at the cell periphery [20]. This effect
is associated with induction of actin polymerization,
because latrunculin B, which F- disrupts actin, com-
pletely blocks it, and, vice versa, increases motility of
mitochondria [19,20]. It was shown in further studies
that the vimentin IFs play a role of a mediator be-
tween the interacting mitochondria and cytoskeleton
actin structures [22].
Using targeted mutagenesis, we were able to
identify the site at the N-terminus of the vimentin
molecule responsible for mitochondria binding [22]
that exhibits properties of signaling sequence for
mitochondria localization [23]. Considering that the
mitochondrial proteins with such signaling sequences
interact with the complexes of mitochondrial trans-
locases [24], it could be suggested that vimentin also
interacts with them. These data attracted significant
attention from many researchers, because it was
known that the functions of mitochondria in many
cells are disrupted in the case of damage of the IF
network [25, 26]. Large amounts of data have been
accumulated on various pathological states associat-
ed with disruption of different types of IFs and, as a
consequence, with defects in mitochondria function-
ing [27-30]. Many authors emphasized the probable
role of IFs in regulation of the properties of mito-
chondria and of the whole cells [31-33], however, at
present there are no sufficient data on connections
of these organelles and on mechanisms underlying
the observed cellular defects to make definite con-
clusions.
VIMENTIN INTERMEDIATE FILAMENTS
ENSURE CELLULAR MITOSTASIS
Unlike in the case of microtubules and actin
microfilaments, which are composed from a limit-
ed number of isoforms of tubulin and actin, respec-
tively, and are practically identical in all eukaryotes,
IFs are represented by one of the numerous protein
families [34]. In the human genome, more than 70
genes encoding various IF proteins were identified
[35], which are expressed depending on the tissue
type and stage of differentiation. Vimentin is unique
among the other IF proteins: in addition to mesen-
chymal cells where it is the only representative of
this family, its expression was found in neurons, epi-
theliocytes, muscle cells, and some other [35], where
it appeared under certain conditions. And, although,
as has been mentioned above, disruption of the func-
tions of mitochondria has been observed in different
cell types with damaged IFs of different composition,
the issue on their ability to bind mitochondria direct-
ly remains open to discussion. At present, direct as-
sociation with mitochondria was demonstrated in our
study only for vimentin [36] and desmin IFs [37], no
data are available for other IFs.
How the vimentin IFs control properties of mi-
tochondria? In addition to limiting motility of mito-
chondria on their binding to vimentin IFs, this in-
teraction results in the increase of the mitochondrial
membrane potential [38]. Interestingly, increase of
the level of membrane potential was observed not
only during restoration of vimentin IFs in the knock-
out cells, but also in the case of expression of the
vimentin fragment containing the mitochondria-bind-
ing site [37]. Association of vimentin IFs with mito-
chondria is under regulatory control. In particular,
it was shown in our study [39] that activation of
the small GTPase Rac1 increases motility mobility of
mitochondria in the mouse fibroblasts 2-fold. It was
found that one of its effectors, protein kinase PAK1,
could participate in vimentin phosphorylation at the
Ser55 residue, and this disrupts its association with
mitochondria. In addition to the increase of motility
of mitochondria upon activation of the GTPase Rac1
and protein kinase PAK1, a decrease in the mitochon-
drial membrane potential was observed. Interestingly,
replacement of Ser with Ala at this position of vimen-
tin molecule blocked the effect of GTPase Rac1 on the
properties of mitochondria [39]. It is likely that there
are other mechanisms regulating this interaction.
In particular, analysis of recombinant vimentin bind-
ing with mitochondria isolated from the rat liver cells
DEEB et al.1914
BIOCHEMISTRY (Moscow) Vol. 90 No. 12 2025
demonstrates that the protein could be subjected to
partial hydrolysis, which is catalyzed by mitochondri-
al proteases [36]. Proteolysis of the N-terminal part of
the vimentin molecules was observed during incuba-
tion in the absence of inhibitors of cysteine proteases,
and their association with mitochondria was disrupt-
ed. The results of inhibitory analysis showed that the
mitochondrial atypical Ca
2+
-dependent calpain prote-
ase is the enzyme responsible for vimentin degrada-
tion. Considering that mitochondrial matrix contains
main fraction of the intracellular Ca
2+
, and its concen-
tration in the intermembrane space of mitochondria
and in cytosol is very low, it could be suggested that
proteolysis is initiated by the decrease of mitochon-
drial potential, when Ca
2+
is excreted [36]. It is likely
that the association of mitochondria with vimentin
IFs is controlled by the mitochondrial potential.
Mitochondrial membrane potential could be
maintained via two pathways: a) operation of mito-
chondrial electron-transport chain of mitochondria;
b) as a result of ATP hydrolysis in the reverse reaction
catalyzed by H-ATPase. Hence, the effect of vimentin
IFs on the level of membrane potential observed in
our study could be caused both by stimulation of
activity of the mitochondrial respiratory chain, and
through the independent pathway involving acceler-
ation of ATP hydrolysis. In order to find out which
of these mechanisms underlie the effect of vimentin,
we used the fibroblast cell line lacking mitochondrial
DNA, and, as a consequence, lacking several import-
ant protein components of the mitochondrial respi-
ratory chain. Potential in these cells is maintained
through hydrolysis of ATP formed in the process
of glycolysis. We demonstrated that restoration of
vimentin IFs in these cells did not result in the in-
crease of potential. And, on the contrary, suppression
of vimentin expression in the cells with disrupted
respiratory chain with the help of RNA interference
did not decrease potential as observed in the initial
cells [38]. Hence, the effect of vimentin IFs on the
mitochondrial membrane potential is observed only
in cells with a fully functional respiratory chain. How
could vimentin affect the operation of the mitochon-
drial respiratory chain?
It was shown previously that mitochondria have
low respiratory activity, increased level of ATP, and
disrupted morphology in the fibroblasts isolated from
the mice with knockout of the vimentin gene [33]. The
authors of this study suggested that the main cause
of disruption of mitochondrial functions is oxidative
stress, and vimentin protects mitochondria against
ROS [33]. However, the causes of the increase of ROS
levels in the mitochondria remain poorly understood.
It was demonstrated recently in the collaborative
study of the laboratories of Russo and Markovitz that
knockout of the vimentin gene in mice causes signifi-
cant changes in the expression of the genes of many
proteins in neutrophils [40]. They found an increase
of expression of 108 genes and decrease of expression
of 416 genes in the cells lacking vimentin in compari-
son with the wild type neutrophils. Significant chang-
es were observed in the expression of the genes par-
ticipating in mitochondria functioning. In particular,
expression of 55 genes encoding proteins of all five
complexes of mitochondrial respiratory chains was
reduced. Hence, vimentin IFs in neutrophils control
protein composition of mitochondria, and, conse-
quently, their properties. Furthermore, it was shown
that deletion of vimentin results in the decrease of
expression of the proteins SOD1 and SOD2 that play
roles of antioxidants [40]. The authors suggested that
exactly these changes were the causes of noticeable
increase of ROS levels in the neutrophils.
It should be mentioned that ROS, which cause
different damages and pathologies, also perform a
number of regulatory functions, and for this, their
concentration should be maintained at a certain lev-
el. Several sources of ROS exist in the cells includ-
ing NADPH-oxidase integrated into the plasma mem-
brane, xanthine oxidase, and mitochondria [41], as
well as the system of antioxidant enzymes. Thus, our
data [42] indicate that peroxide formed in mitochon-
dria stimulates migration of fibroblasts. Hence, it is
likely that vimentin IFs not only decrease the level of
ROS but also participate in stabilization of its level.
On the other hand, vimentin ensures enhanced re-
sistance of mitochondria to oxidative stress [43] and
to action of anti-cancer preparations doxorubicin and
vincristine [44]. This protective effect could indicate
not only decrease of the ROS level but also changes
in the mitochondria properties caused by interaction
with vimentin. This suggestion is supported by the
fact that expression of the vimentin mutant with
disrupted ability to bind mitochondria did not pro-
vide protective effect in the cells [42, 43]. Hence, the
protective effect of vimentin depends on its ability
to bind mitochondria. However, binding of vimentin
IFs with mitochondria has not been investigated in
sufficient detail, although there are data indicating
that regulation of the mitochondria interaction with
vimentin IFs could be realized both directly and in-
directly. The ITPRIPL2 protein co-localized with vi-
mentin could play a role of a mediator [45]; knock-
down of this protein disrupts processing of vimentin
and formation of IFs and plectin 1b [46]. It was also
shown that the microRNA miR-124 regulates vimentin
expression and indirectly controls motility of mito-
chondria [47].
Based on the data obtained in our study [22],
the site of vimentin molecule responsible for inter-
action is located in the N-terminal part of the mole-
cule, and its composition is similar to the localization
MITOSTASIS – FOCUS ON VIMENTIN FILAMENTS 1915
BIOCHEMISTRY (Moscow) Vol. 90 No. 12 2025
Fig. 2. Effects of vimentin IFs on mitochondria that maintain their homeostasis: binding of mitochondria to the network
of IFs limits their motility and determines their intracellular distribution (shown in green color); maintenance of high
mitochondrial membrane potential and decrease of ROS concentration (shown in blue color); increase of resistance of mito-
chondria to oxidative stress and to the action of cytostatic agents, and protection against apoptosis (shown in orange color).
signal typical of many mitochondrial proteins. Hence,
vimentin could bind to the mitochondrial translocas-
es TOM/TIM responsible for import of proteins con-
taining these sequences. However, accessibility of
the N-terminal domain in vimentin could be limited.
According to the recent data reported by the Medalia
research group obtained with the help of cryo-elec-
tron microscopy and tomography [48], the vimentin
IFs comprise a cylindrical structure formed by five
protofibrils, each composed of 40 alpha-helices of the
vimentin central domain. The non-structured C-termi-
nal parts are located outside and stabilize bonds be-
tween the protofibrils, while the N-terminal domains
are in the inner cavity of the filament and form a
rather compact bundle also creating additional bonds
between the individual components. Hence, the N-ter-
minal domain site responsible for mitochondria bind-
ing turns out to be hidden inside the filament. It can
be assumed that mitochondria bind to this part of
the vimentin molecule at the terminal parts of the
filaments, where the cylindrical structure is not fully
formed. Otherwise, significant rearrangements of the
vimentin IFs would be required to allow external ex-
posure of the N-terminal sites.
CONCLUSIONS
In conclusion, it could be stated that among the
three components of cytoskeleton, the vimentin IFs
are the most suitable candidates capable of maintain-
ing mitostasis. They could play a role of organizers
of intracellular space, and this organization is vital –
abundant evidence exists on different pathological
states associated with disruptions of the IF structure,
which cause defects in the mitochondria functioning.
The data on participation of vimentin in reg-
ulation of the properties of mitochondria provide
grounds to assumptions that the vimentin IF could
contribute to mitostasis maintenance. A number of
factors, both structural and functional, indicate their
involvement in realization and maintenance of nor-
mal functioning of mitochondria. In particular, vimen-
tin filaments interact with mitochondria; this interac-
tion could be direct or through the protein mediators.
Vimentin filaments regulate motility of mitochondria;
they are capable of stabilizing mitochondria and pro-
tecting them against apoptosis and stress. And, final-
ly, vimentin filaments could affect the mitochondrial
potential (Fig. 2).
By regulating mitochondrial functions, vimentin
IFs could significantly affect properties of the whole
cells: the cells expressing vimentin, unlike other cells,
have the ability to migrate over significant distanc-
es, they exhibit increased resistance to the action of
cytostatics, and are less susceptible to apoptosis un-
der unfavorable conditions. From this point of view,
vimentin filaments could be considered as a target
for normalization of mitostasis in the case of its dis-
ruption under the action of external or internal nega-
tive factors. This fundamentally novel approach could
offer a new solution to the problem of treating nu-
merous human diseases associated with disruptions
of mitochondria functions.
DEEB et al.1916
BIOCHEMISTRY (Moscow) Vol. 90 No. 12 2025
Abbreviations
IF intermediate filaments
ROS reactive oxygen species
Contributions
I. B. Alieva and A. A. Minin – concept and supervi-
sion of the study, discussion of the results; R. Deeb,
A. S. Churkina, I. B. Alieva, A. S. Shakhov, and
A. A. Minin – writing text of the paper; A. S. Shak-
hov and A. S. Churkina – preparation of illustrations;
I. B. Alieva and A. A. Minin – editing text of the paper.
Funding
This study was financially supported by the Russian
Science Foundation (grant no.23-74-00036).
Ethics approval and consent to participate
This work does not contain any studies involving
human and animal subjects.
Conflict of interest
The authors of this work declare that they have
noconflicts of interest.
REFERENCES
1. Walkon, L. L., Strubbe-Rivera, J. O., and Bazil, J. N.
(2022) Calcium overload and mitochondrial metab-
olism, Biomolecules, 12, 1891, https://doi.org/10.3390/
biom12121891.
2. Melchinger,P., and Garcia, B.M. (2023) Mitochondria
are midfield players in steroid synthesis, Int. J. Bio-
chem. Cell Biol., 160, 106431, https://doi.org/10.1016/
j.biocel.2023.106431.
3. Gulbins, E., Dreschers,S., and Bock, J. (2003) Role of
mitochondria in apoptosis, Exp. Physiol., 88, 85-90,
https://doi.org/10.1113/eph8802503.
4. Skulachev, V. P., Bakeeva, L. E., Chernyak, B. V.,
Domnina, L. V., Minin, A. A., Pletjushkina, O. Y.,
Saprunova, V. B., Skulachev, I. V., Tsyplenkova,
V. G., Vasiliev, J. M., Yaguzhinsky, L. S., and Zorov,
D. B. (2004) Thread-grain transition of mitochon-
drial reticulum as a step of mitoptosis and apop-
tosis, Mol. Cell. Biochem., 256-257, 341-358, https://
doi.org/10.1023/b:mcbi.0000009880.94044.49.
5. Godoy, J. A., Rios, J. A., Picón-Pagès, P., Herrera-
Fernández, V., Swaby, B., Crepin, G., Vicente, R.,
Fernández-Fernández, J. M., and Muñoz, F. J. (2021)
Mitostasis, calcium and free radicals in health, ag-
ing and neurodegeneration, Biomolecules, 11, 1012,
https://doi.org/10.3390/biom11071012.
6. Misgeld, T., and Schwarz, T. L. (2017) Mitostasis in
neurons: maintaining mitochondria in an extended
cellular architecture, Neuron, 96, 651-666, https://
doi.org/10.1016/j.neuron.2017.09.055.
7. Sies, H., and Jones, D. P. (2020) Reactive oxygen
species (ROS) as pleiotropic physiological signalling
agents, Nat. Rev. Mol. Cell Biol., 21, 363-383, https://
doi.org/10.1038/s41580-020-0230-3.
8. Varesi, A., Chirumbolo, S., Campagnoli, L. I. M.,
Pierella, E., Piccini, G. B., Carrara, A., Ricevuti, G.,
Scassellati, C., Bonvicini, C., and Pascale, A. (2022)
The role of antioxidants in the interplay between
oxidative stress and senescence, Antioxidants, 11,
1224, https://doi.org/10.3390/antiox11071224.
9. Guéraud, F., Atalay, M., Bresgen, N., Cipak, A., Eckl,
P. M., Huc, L., Jouanin, I., Siems, W., and Uchida, K.
(2010) Chemistry and biochemistry of lipid perox-
idation products, Free Radic. Res., 44, 1098-1124,
https://doi.org/10.3109/10715762.2010.498477.
10. Viedma-Poyatos,Á., González-Jiménez,P., Langlois,O.,
Company-Marín, I., Spickett, C. M., and Pérez-
Sala, D. (2021) Protein lipoxidation: Basic concepts
and emerging roles, Antioxidants, 10, 295, https://
doi.org/10.3390/antiox10020295.
11. Di Lorenzo, R., Chimienti, G., Picca, A., Trisolini, L.,
Latronico, T., Liuzzi, G. M., Pesce, V., Leeuwen-
burgh, C., and Lezza, A. M. S. (2024) Resveratrol
impinges on retrograde communication without in-
ducing mitochondrial biogenesis in aged rat soleus
muscle, Exp. Gerontol., 194, 112485, https://doi.org/
10.1016/j.exger.2024.112485.
12. Fernández Casafuz, A. B., De Rossi, M. C., and
Bruno, L. (2023) Mitochondrial cellular organiza-
tion and shape fluctuations are differentially mod-
ulated by cytoskeletal networks, Sci. Rep., 13, 4065,
https://doi.org/10.1038/s41598-023-31121-w.
13. Boldogh, I. R., and Pon, L. A. (2006) Interactions of
mitochondria with the actin cytoskeleton, Biochim.
Biophys. Acta, 1763, 450-462, https://doi.org/10.1016/
j.bbamcr.2006.02.014.
14. Saxton, W.M., and Hollenbeck, P.J. (2012) Theaxonal
transport of mitochondria, J.Cell Sci., 125, 2095-2104,
https://doi.org/10.1242/jcs.053850.
15. Mooseker, M. S., and Cheney, R. E. (1995) Unconven-
tional myosins, Annu. Rev. Cell Dev. Biol., 11, 633-
675, https://doi.org/10.1146/annurev.cb.11.110195.
003221.
16. Taunton, J., Rowning, B. A., Coughlin, M. L.,
Wu, M., Moon, R. T., Mitchison, T. J., and Larabell,
C. A. (2000) Actin-dependent propulsion of endo-
somes and lysosomes by recruitment of N-WASP,
J. Cell Biol., 148, 519-530, https://doi.org/10.1083/jcb.
148.3.519.
17. Kulik, A. V., Gioeva, F. K., and Minin, A. A. (2002)
Study of mitochondria movement using videomicros-
copy [in Russian], Ontogenez, 33, 366-373.
18. Nekrasova, O. E., Minin, An. A., Kulik, A. V., and
Minin, A. A. (2005) Regulation of shape and distri-
bution of mitochondria by fibronectin [in Russian],
Biol. Membr., 22, 105-112.
MITOSTASIS – FOCUS ON VIMENTIN FILAMENTS 1917
BIOCHEMISTRY (Moscow) Vol. 90 No. 12 2025
19. Kulik, A.V., Nekrasova, O.E., and Minin, A.A. (2006)
Mitochondria motility is regulated by F-actin [in Rus-
sian], Biol. Membr., 23, 42-51.
20. Minin, A. A., Kulik, A. V., Gyoeva, F. K., Li, Y.,
Goshima,G., and Gelfand, V.I. (2006) Regulation of mi-
tochondria distribution by RhoA and formins, J. Cell
Sci., 119, 659-670, https://doi.org/10.1242/jcs.02762.
21. Nekrasova, O.E., Kulik, A.V., and Minin, A.A. (2007)
Protein kinase C regulates mitochondrial motility [in
Russian], Biol. Membr., 24, 126-132.
22. Nekrasova, O. E., Mendez, M. G., Chernoivanenko,
I.S., Tyurin-Kuzmin, P.A., Kuczmarski, E.R., Gelfand,
V. I., Goldman, R. D., and Minin, A. A. (2011) Vimen-
tin intermediate filaments modulate the motility of
mitochondria, Mol. Biol. Cell, 22, 2282-2289, https://
doi.org/10.1091/mbc.E10-09-0766.
23. Rapaport, D. (2003) Finding the right organelle Tar-
geting signals in mitochondrial outer-membrane
proteins, EMBO Rep., 4, 948-952, https://doi.org/
10.1038/sj.embor.embor937.
24. Araiso,Y., Imai,K., and Endo,T. (2022) Role of the TOM
complex in protein import into mitochondria: struc-
tural views, Annu. Rev. Biochem., 91, 679-703, https://
doi.org/10.1146/annurev-biochem-032620-104527.
25. Schwarz, N., and Leube, R. E. (2016) Intermediate
filaments as organizers of cellular space: how they
affect mitochondrial structure and function, Cells, 5,
30, https://doi.org/10.3390/cells5030030.
26. Etienne-Manneville, S. (2018) Cytoplasmic inter-
mediate filaments in cell biology, Annu. Rev. Cell
Dev. Biol., 34, 1-28, https://doi.org/10.1146/annurev-
cellbio-100617-062534.
27. Gilbert, S., Loranger, A., Daigle, N., and Marceau, N.
(2001) Simple epithelium keratins 8 and 18 pro-
vide resistance to Fas-mediated apoptosis. The pro-
tection occurs through a receptor-targeting mod-
ulation, J. Cell Biol., 154, 763-773, https://doi.org/
10.1083/jcb.200102130.
28. Capetanaki, Y. (2002) Desmin cytoskeleton: a po-
tential regulator of muscle mitochondrial behavior
and function, Trends Cardiovasc. Med., 12, 339-348,
https://doi.org/10.1016/S1050-1738(02)00184-6.
29. Uttam, J., Hutton, E., Coulombe, P. A., Anton-
Lamprecht, I., Yu, Q. C., Gedde-Dahl, T., Jr., Fine,
J. D., and Fuchs, E. (1996) The genetic basis of epi-
dermolysis bullosa simplex with mottled pigmen-
tation, Proc. Natl. Acad. Sci. USA, 93, 9079-9084,
https://doi.org/10.1073/pnas.93.17.9079.
30. Brownlees, J., Ackerley, S., Grierson, A. J., Jacobsen,
N. J., Shea, K., Anderton, B. H., Leigh, P. N., Shaw,
C.E., and Miller, C.C. (2002) Charcot-Marie-Tooth dis-
ease neurofilament mutations disrupt neurofilament
assembly and axonal transport, Hum. Mol. Genet., 11,
2837-2844, https://doi.org/10.1093/hmg/11.23.2837.
31. Milner, D.J., Mavroidis, M., Weisleder, N., and Capet-
anaki,Y. (2000) Desmin cytoskeleton linked to muscle
mitochondrial distribution and respiratory function,
J. Cell Biol., 150, 1283-1298, https://doi.org/10.1083/
jcb.150.6.1283.
32. Wagner, O. I., Lifshitz, J., Janmey, P. A., Linden, M.,
McIntosh, T. K., and Leterrier, J. F. (2003) Mecha-
nisms of mitochondria-neurofilament interactions,
J. Neurosci., 23, 9046-9058, https://doi.org/10.1523/
JNEUROSCI.23-27-09046.2003.
33. Tolstonog, G.V., Belichenko-Weitzmann, I.V., Lu, J.P.,
Hartig, R., Shoeman, R. L., Traub, U., and Traub, P.
(2005) Spontaneously immortalized mouse embryo
fibroblasts: growth behavior of wild-type and vi-
mentin-deficient cells in relation to mitochondrial
structure and activity, DNA Cell Biol., 24, 680-709,
https://doi.org/10.1089/dna.2005.24.680.
34. Fuchs,E., and Weber,K. (1994) Intermediate filaments:
structure, dynamics, function and disease, Annu. Rev.
Biochem., 63, 345-382, https://doi.org/10.1146/annurev.
bi.63.070194.002021.
35. Alieva, I. B., Shakhov, A. S., Dayal, A. A., Parfenteva,
O. I., and Minin, A. A. (2024) Unique role of vimen-
tin in the intermediate filament proteins family,
Biochemistry (Moscow), 89, 726-736, https://doi.org/
10.1134/S0006297924040114.
36. Dayal, A.A., Medvedeva, N.V., and Minin, A.A. (2022)
N-Terminal fragment of vimentin is responsible for
binding of mitochondria in vitro, Membr. Cell Biol.,
5, 21-28.
37. Dayal, A. A., Medvedeva, N. V., Nekrasova, T. M.,
Duhalin, S.D., Surin, A.K., and Minin, A.A. (2020) De-
smin interacts directly with mitochondria, Int.J. Mol.
Sci., 21, 8122, https://doi.org/10.3390/ijms21218122.
38. Chernoivanenko, I. S., Matveeva, E. A., Gelfand, V. I.,
Goldman, R. D., and Minin, A. A. (2015) Mitochon-
drial membrane potential is regulated by vimentin
intermediate filaments, FASEB J., 29, 820-827, https://
doi.org/10.1096/fj.14-259903.
39. Matveeva, E. A., Venkova, L. S., Chernoivanenko,
I.S., and Minin, A.A. (2015) Vimentin is involved in
regulation of mitochondrial motility and membrane
potential by Rac1, Biol. Open., 4, 1290-1297, https://
doi.org/10.1242/bio.013326.
40. Huynh, T. N., Toperzer, J., Scherer, A., Gumina, A.,
Brunetti, T., Mansour, M. K., Markovitz, D. M., and
Russo, B. C. (2024) Vimentin regulates mitochondri-
al ROS production and inflammatory responses of
neutrophils, Front. Immunol., 15, 1416275, https://
doi.org/10.3389/fimmu.2024.1416275.
41. San Martín, A., and Griendling, K. K. (2010) Redox
control of vascular smooth muscle migration, Antiox-
id. Redox Signal., 12, 625-640, https://doi.org/10.1089/
ars.2009.2852.
42. Venkova, L.S., Chernoivanenko, I.S., and Minin, A.A.
(2014) Hydrogen peroxide stimulating migration of
fibroblasts is formed in mitochondria, Membr. Cell Biol.,
8, 309-313, https://doi.org/10.1134/S1990747814050080.
DEEB et al.1918
BIOCHEMISTRY (Moscow) Vol. 90 No. 12 2025
43. Matveeva, E. A., Chernoivanenko, I. S., and Minin,
A. A. (2010) Vimentin intermediate filaments pro-
tect mitochondria from oxidative stress, Mem-
br. Cell Biol., 4, 321-331, https://doi.org/10.1134/
S199074781004001X.
44. Venkova, L. S., Zerkalenkova, E. A., and Minin, A. A.
(2018) Vimentin protects cells against doxorubi-
cin and vincristine, Membr. Cell Biol., 12, 255-260,
https://doi.org/10.1134/S1990747818030091.
45. Hemel, I. M. G. M., Steen, C., Denil, S. L. I. J., Ertay-
lan, G., Kutmon, M., Adriaens, M., and Gerards, M.
(2025) The unusual suspect: A novel role for inter-
mediate filament proteins in mitochondrial mor-
phology, Mitochondrion, 81, 102008, https://doi.org/
10.1016/j.mito.2025.102008.
46. Winter, L., Abrahamsberg, C., and Wiche, G. (2008)
Plectin isoform 1b mediates mitochondrion-inter-
mediate filament network linkage and controls
organelle shape, J. Cell Biol., 181, 903-911, https://
doi.org/10.1083/jcb.200710151.
47. Yardeni, T., Fine, R., Joshi, Y., Gradus-Pery, T.,
Kozer, N., Reichenstein, I., Yanowski, E., Nevo, S.,
Weiss- Tishler, H., Eisenberg-Bord, M., Shalit, T.,
Plotnikov, A., Barr, H. M., Perlson, E., and Horn-
stein, E. (2018) High content image analysis reveals
function of miR-124 upstream of Vimentin in regu-
lating motor neuron mitochondria, Sci. Rep., 8, 59,
https://doi.org/10.1038/s41598-017-17878-x.
48. Eibauer, M., Weber, M. S., Kronenberg-Tenga, R.,
Beales, C. T., Boujemaa Paterski, R., Turgay, Y.,
Sivagurunathan, S., Kraxner, J., Koster, S., Goldman,
R. D., and Medalia, O. (2024) Vimentin filaments in-
tegrate low complexity domains in a complex he-
lical structure, Nat. Struct. Mol. Biol., 31, 939-949,
https://doi.org/10.1038/s41594-024-01261-2.
Publisher’s Note. Pleiades Publishing remains
neutral with regard to jurisdictional claims in published
maps and institutional affiliations. AI tools may have
been used in the translation or editing of this article.
