REVIEW: EB-Family Proteins: Functions and Microtubule Interaction Mechanisms

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V. V. Mustyatsa¹, A. V. Boyakhchyan², F. I. Ataullakhanov^1,2,3, and N. B. Gudimchuk^1,2,3*

¹Dmitry Rogachev National Scientific and Practical Center of Pediatric Hematology, Oncology, and Immunology, 117997 Moscow, Russia

²Center for Theoretical Problems of Physico-Chemical Pharmacology, Russian Academy of Sciences, 119991 Moscow, Russia

³Lomonosov Moscow State University, Faculty of Physics, 119991 Moscow, Russia; E-mail: gudimchuk@phys.msu.ru

^* To whom correspondence should be addressed.

Received March 20, 2017; Revision received April 6, 2017

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Microtubules are polymers of tubulin protein, one of the key components of cytoskeleton. They are polar filaments whose plus-ends usually oriented toward the cell periphery are more dynamic than their minus-ends, which face the center of the cell. In cells, microtubules are organized into a network that is being constantly rebuilt and renovated due to stochastic switching of its individual filaments from growth to shrinkage and back. Because of these dynamics and their mechanical properties, microtubules take part in various essential processes, from intracellular transport to search and capture of chromosomes during mitosis. Microtubule dynamics are regulated by many proteins that are located on the plus-ends of these filaments. One of the most important and abundant groups of plus-end-interacting proteins are EB-family proteins, which autonomously recognize structures of the microtubule growing plus-ends, modulate their dynamics, and recruit multiple partner proteins with diverse functions onto the microtubule plus-ends. In this review, we summarize the published data about the properties and functions of EB-proteins, focusing on analysis of their mechanism of interaction with the microtubule growing ends.

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KEY WORDS: microtubules, dynamic microtubules, EB-proteins

DOI: 10.1134/S0006297917070045

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