REVIEW: Three-Finger Proteins from the Ly6/uPAR Family: Functional Diversity within One Structural Motif

---

N. A. Vasilyeva^1,2,3, E. V. Loktyushov^1,2, M. L. Bychkov², Z. O. Shenkarev², and E. N. Lyukmanova^1,2*

¹Lomonosov Moscow State University, Faculty of Biology, 119991 Moscow, Russia; E-mail: ekaterina-lyukmanova@yandex.ru

²Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia

³Institute of Higher Nervous Activity and Neurophysiology, Russian Academy of Sciences, 117485 Moscow, Russia

^* To whom correspondence should be addressed.

Received September 7, 2017

---

The discovery in higher animals of proteins from the Ly6/uPAR family, which have structural homology with snake “three-finger” neurotoxins, has generated great interest in these molecules and their role in the functioning of the organism. These proteins have been found in the nervous, immune, endocrine, and reproductive systems of mammals. There are two types of the Ly6/uPAR proteins: those associated with the cell membrane by GPI-anchor and secreted ones. For some of them (Lynx1, SLURP-1, SLURP-2, Lypd6), as well as for snake α-neurotoxins, the target of action is nicotinic acetylcholine receptors, which are widely represented in the central and peripheral nervous systems, and in many other tissues, including epithelial cells and the immune system. However, the targets of most proteins from the Ly6/uPAR family and the mechanism of their action remain unknown. This review presents data on the structural and functional properties of the Ly6/uPAR proteins, which reveal a variety of functions within a single structural motif.

---

KEY WORDS: three-finger proteins, nicotinic acetylcholine receptor, Ly6/uPAR, Lynx1, Lypd6, SLURP

DOI: 10.1134/S0006297917130090

---