Microtubule: a dynamically unstable stochastic phase switching polymer

Zakharov, Pavel N.; Arzhanik, Vladimir K.; Ulyanov, Evgenii V.; Gudimchuk, Nikita; Ataullakhanov, Fazoil I.

doi:10.3367/ufnr.2016.04.037779

Cited by 6 publications

(2 citation statements)

References 104 publications

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“…They form cilia and flagella and serve as tracks for long-distance transport of intracellular cargos, such as vesicles and organelles. In contrast to other polymers, microtubules are highly non-equilibrium systems [2], which can remain in growth and shrinkage phases with relatively rare spontaneous transitions between them [3]. Because of this behavior, known as dynamic instability, individual microtubules display significant length changes, even at steady state.…”

Section: Introductionmentioning

confidence: 99%

Mechanical properties of tubulin intra- and inter-dimer interfaces and their implications for microtubule dynamic instability

et al. 2019

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Thirteen tubulin protofilaments, made of αβ-tubulin heterodimers, interact laterally to produce cytoskeletal microtubules. Microtubules exhibit the striking property of dynamic instability, manifested in their intermittent growth and shrinkage at both ends. This behavior is key to many cellular processes, such as cell division, migration, maintenance of cell shape, etc. Although assembly and disassembly of microtubules is known to be linked to hydrolysis of a guanosine triphosphate molecule in the pocket of β-tubulin, detailed mechanistic understanding of corresponding conformational changes is still lacking. Here we take advantage of the recent generation of in-microtubule structures of tubulin to examine the properties of protofilaments, which serve as important microtubule assembly and disassembly intermediates. We find that initially straight tubulin protofilaments, relax to similar non-radially curved and slightly twisted conformations. Our analysis further suggests that guanosine triphosphate hydrolysis primarily affects the flexibility and conformation of the inter-dimer interface, without a strong impact on the shape or flexibility of αβ-heterodimer. Inter-dimer interfaces are significantly more flexible compared to intra-dimer interfaces. We argue that such a difference in flexibility could be key for distinct stability of the plus and minus microtubule ends. The higher flexibility of the inter-dimer interface may have implications for development of pulling force by curving tubulin protofilaments during microtubule disassembly, a process of major importance for chromosome motions in mitosis.

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Section: Introductionmentioning

confidence: 99%

Mechanical properties of tubulin intra- and inter-dimer interfaces and their implications for microtubule dynamic instability

et al. 2019

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“…While the stabilizing cap is present at the MT tip, the MT can grow. When the stabilizing cap is lost due to stochastic GTP hydrolysis, or dissociation of GTP-tubulins, or loss of lateral bonds between them, MTs switch to the shrinkage (Zakharov et al , 2016). The structure and dynamics of the stabilizing cap, however, have remained elusive because of the lack of direct methods to visualize it.…”

Section: Introductionmentioning

confidence: 99%

Fine structure and dynamics of EB3 binding zones on microtubules in fibroblast cells

Mustyatsa

Kostarev

Tvorogova

et al. 2019

MBoC

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End-binding (EB) proteins associate with the growing tips of microtubules (MTs)and modulate their dynamics directly and indirectly, by recruiting essential factors to fine-tune MTs for their many essential roles in cells. Previously EB proteins have been shown to recognize a stabilizing GTP/GDP-Pi cap at the tip of growing MTs, but information about additional EB-binding zones on MTs has been limited. In this work, we studied fluorescence intensity profiles of one of the three mammalian EB-proteins, EB3, fused with red fluorescent protein (RFP). The distribution of EB3 on MTs in mouse fibroblasts frequently deviated from single exponential decay and exhibited secondary peaks. Those secondary peaks, which we refer to as EB3-islands, were detected on 56% comets of growing MTs and were encountered once per 44 s of EB3-RFP comet growth time with about 5 s half-lifetime. The majority of EB3-islands in the vicinity of MT tips was stationary and originated from EB3 comets moving with the growing MT tips. Computational modeling of the decoration of dynamic MT tips by EB3 suggested that the EB3-islands could not be explained simply by a stochastic first-order GTP hydrolysis/phosphate release. We speculate that additional protein factors contribute to EB3 residence time on MTs in cells, likely affecting MT dynamics.

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About Biophysics and the Chair of Biophysics at the Faculty of Physics of Moscow State University

Tverdislov,

Lobyshev,

Yakovenko

et al. 2023

BIOPHYSICS

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Microtubule: a dynamically unstable stochastic phase switching polymer

Cited by 6 publications

References 104 publications

Mechanical properties of tubulin intra- and inter-dimer interfaces and their implications for microtubule dynamic instability

Mechanical properties of tubulin intra- and inter-dimer interfaces and their implications for microtubule dynamic instability

Fine structure and dynamics of EB3 binding zones on microtubules in fibroblast cells

About Biophysics and the Chair of Biophysics at the Faculty of Physics of Moscow State University

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