Vladimir Volkov


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Research experience


Delft University of Technology, Marileen Dogterom lab
Delft, The Netherlands


In an ongoing a collaborative project with the lab of Andrea Musacchio, we aim at reconstitution of the force-generating interface between a microtubule end and a reconstituted human kinetochore.

Microtubules exert forces on kinetochores to generate tension and movement. Correctly attached microtubules must be stabilized to prevent their detachment, while other microtubules must be destabilized and let detach. Recently we have established how force-coupling properties of this interface are regulated by mitotic kinases. We identified the duration of the kinetochore-mediated stall in microtubule shortening to be a fundamental parameter, which determines whether a microtubule will detach (after a stall shorter than 1 second) or convert to growh, in other words rescue (after a stall longer than 1 second). Phosphorylation of Ndc80 complex by Aurora B kinase leads to shorter stalls and promotes detachment. Phosphorylation of Ska complex by Cdk1 kinase enables it to interact with Ndc80, providing an additional microtubule-binding site and leading to longer stalls and rescues [1].
stall duration defines attachment outcome

Previously, we employed precisely oligomerized full-length human Ndc80 complexes as a tool to demonstrate that Ndc80 does not need additional kinetochore components to stall a depolymerizing microtubule end and rescue its shortening in a force-dependent manner [5]. My data suggest that only in the context of oligomers joined at the kinetochore-binding side, the Ndc80 complex acquires an ability to interact with the flared protofilaments at the microtubule tip. in vitro reconstitution of microtubule-kinetochore interaction

I also contributed to the collaborative projects directed at understanding how the microtubule-generated forces remodel cellular membranes[2] and how the microtubule depolymerase MCAK is regulated[3]


Russian academy of sciences/Gamaleya Research Institute for
Epidemiology and Microbiology, Moscow, Russia
Semi-independent position


I have lead a small research group studying the properties of human Centromere protein F (CENP-F) as a coupler of microtubule dynamics to motility of cargo. Using in vitro reconstitution we have demonstrated the role of N- and C-terminal microtubule-binding sites of CENP-F in coupling the motility of cellular cargos to both growing and shortening microtubule tips. Our results highlight the potential role of CENP-F in initial capture of chromosomes in prometaphase [6], and in redistribution of mitochondrial network after mitosis [5].
Beads coated with CENP-F follow growth and shrinkage of microtubules
I had to leave this position and continue my postdoc because in 2015 the Dmitry Zimin Dynasty Foundation, my main funder, was forced by Russian government to cease its operation. Apart from loss of funding, this was a signal for me that groups collaborating with western labs are no longer welcome in Russia.

PhD student

University of Colorado/Russian academy of sciences
Richard McIntosh/Fazly Ataullakhanov labs


I was enrolled in graduate school in Moscow, Russia in the lab of Fazly Ataullakhanov. The actual research was done in the University of Colorado at Boulder, CO, USA as a collaboration project with the lab of Richard McIntosh. In the lab of Prof. Richard McIntosh I have shown for the first time that Ndc80 complex is able to transport a cargo with the end of depolymerizing microtubule in vitro [10]. I have also contributed to studies that showed that ring formation is not necessary for the coupling of microtubule ends to the budding yeast Dam1 complex [11-12]. Ndc80-coated bead follows microtubule shortening

My following project was dedicated to the effect of the coupler's geometry on the amount of force measured at the depolymerizing microtubule end. I have shown that the presence of long tethers between the bead cargo and the microtubule-tracking Dam1 ring dramatically increases the force measured using the optical trap [8]. Geometry of cargo attachment to the microtubule influences the measured force


Research center for hematology, Moscow, Russia


I used primary hepatocytes isolated from mice and rats to establish the functions of two isoforms of methionine adenosyl transferase, MATI and MATIII. I found that MATI, an isoform with slower kinetics, acts at low methionine concentrations, but it switches to a faster enzyme, MATIII, when methionine concentration rises [13]. AdoMet and methionine consumption rate in primary hepatocytes rise nonlinearly with increased methionine concentraion


Undergraduate student

Research center for hematology, Moscow, Russia


I developed an HPLC method for determination of vincristine concentration in the blood samples of oncological patients.


1. Microtubules pull the strings: disordered sequences as efficient couplers of microtubule-generated force

VA VolkovEssays in Biochemistry 2020; EBC20190078. DOI: 10.1042/EBC20190078

2. Mechanisms of motor-independent membrane remodeling driven by dynamic microtubules

R Rodríguez-García, VA Volkov, C-Y Chen, EA Katrukha, N Olieric, A Aher, I Grigoriev, MP López, MO Steinmetz, LC Kapitein, G Koenderink, M Dogterom, A Akhmanova. Current Biology 2020; 30(6): 972-987.e12. DOI: 10.1016/j.cub.2020.01.036
preprint: bioRxiv

3. Molecular determinants of the Ska-Ndc80 interaction and their influence on microtubule tracking and force-coupling

PJ Huis in ’t Veld*, VA Volkov*, I Stender, A Musacchio, M Dogterom. eLife 2019; 8:e49539 DOI: 10.7554/eLife.49539
preprint: bioRxiv
*equal contribution

4. The depolymerase activity of MCAK shows graded response to Aurora B kinase phosphorylation through allosteric regulation

T McHugh, J Zou, VA Volkov, SK Talapatra, J Rappsilber, M Dogterom, JPI Welburn. Journal of Cell Science 2019; 132(4): jcs.228353 DOI: 10.1242/jcs.228353

5. Multivalency of NDC80 in the outer kinetochore is essential to track shortening microtubules and generate forces

VA Volkov*, PJ Huis in ’t Veld*, M Dogterom, A Musacchio. eLife 2018; 7:e36764 DOI: 10.7554/eLife.36764
preprint: bioRxiv
*equal contribution

6. CENP-F couples cargo to growing and shortening microtubule ends

G Kanfer, M Peterka, VK Arzhanik, AL Drobyshev, FI Ataullakhanov, VA Volkov*, B Kornmann*. Molecular biology of the cell (2017) 28(18), 2400-2409
DOI: 10.1091/mbc.e16-11-0756
preprint: bioRxiv
*equal contribution, co-corresponding authors

7. Centromere protein F includes two sites that couple efficiently to depolymerizing microtubules

VA Volkov, PM Grissom, VK Arzhanik, AV Zaytsev, K Renganathan, T McClure-Begley, WM Old, N Ahn, JR McIntosh. Journal of Cell Biology (2015) 209(6), 813-828 DOI: 10.1083/jcb.201408083
This paper was highlighted in F1000.

8. Preparation of segmented microtubules to study motions driven by the disassembling microtubule ends

VA Volkov, AV Zaytsev, EL Grishchuk. Journal of of visualized experiments: JoVE (2014) 85
full text and video protocol

9. Long tethers provide high-force coupling of the Dam1 ring to shortening microtubules

VA Volkov, AV Zaytsev, N Gudimchuk, PM Grissom, AL Gintsburg, FI Ataullakhanov, JR McIntosh, EL Grishchuk. Proceedings of the National Academy of Sciences (2013) 110(19), 7708-7713 DOI: 10.1073/pnas.1305821110

10. Tubulin depolymerization may be an ancient biological motor

JR McIntosh, V Volkov, FI Ataullakhanov, EL Grishchuk. Journal of Cell Science (2010) 123(20), 3425-3434 DOI: 10.1242/jcs.067611

11. Fibrils connect microtubule tips with kinetochores: a mechanism to couple tubulin dynamics to chromosome motion

JR McIntosh, EL Grishchuk, MK Morphew, AK Efremov, K Zhudenkov, VA Volkov, IM Cheeseman, A Desai, DN Mastronarde, FI Ataullakhanov. Cell (2008) 135(2), 322-333 DOI: 10.1016/j.cell.2008.08.038

12. The Dam1 ring binds microtubules strongly enough to be a processive as well as energy-efficient coupler for chromosome motion

EL Grishchuk, AK Efremov, VA Volkov, IS Spiridonov, N Gudimchuk, S Westermann, D Drubin, G Barnes, JR McIntosh, FI Ataullakhanov. Proceedings of the National Academy of Sciences (2008) 105(40), 15423-15428 DOI: 10.1073/pnas.0807859105

13. Different assemblies of the DAM1 complex follow shortening microtubules by distinct mechanisms

EL Grishchuk, IS Spiridonov, VA Volkov, AK Efremov, S Westermann, D Drubin, G Barnes, FI Ataullakhanov, JR McIntosh. Proceedings of the National Academy of Sciences (2008) 105(19), 6918-6923 DOI: 10.1073/pnas.0801811105

14. An allosteric mechanism for switching between parallel tracks in mammalian sulfur metabolism

TK Korendyaseva, DN Kuvatov, VA Volkov, MV Martinov, VM Vitvitsky, R Banerjee, FI Ataullakhanov. PLoS computational biology (2008) 4(5), e1000076 DOI: 10.1371/journal.pcbi.1000076

Vladimir Volkov — v.volkov@tudelft.nl — +31 15 278-4058 — @microtubule_guy