Dogterom Marileen

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Last Name
Dogterom
First Name
Marileen
ORCID
0000-0002-8803-5261

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  • Article
    Mammalian end binding proteins control persistent microtubule growth
    (Rockefeller University Press, 2009-03-02) Komarova, Yulia A. ; De Groot, Christian O. ; Grigoriev, Ilya ; Gouveia, Susana Montenegro ; Munteanu, E. Laura ; Schober, Joseph M. ; Honnappa, Srinivas ; Buey, Ruben M. ; Hoogenraad, Casper C. ; Dogterom, Marileen ; Borisy, Gary G. ; Steinmetz, Michel O. ; Akhmanova, Anna
    End binding proteins (EBs) are highly conserved core components of microtubule plus-end tracking protein networks. Here we investigated the roles of the three mammalian EBs in controlling microtubule dynamics and analyzed the domains involved. Protein depletion and rescue experiments showed that EB1 and EB3, but not EB2, promote persistent microtubule growth by suppressing catastrophes. Furthermore, we demonstrated in vitro and in cells that the EB plus-end tracking behavior depends on the calponin homology domain but does not require dimer formation. In contrast, dimerization is necessary for the EB anti-catastrophe activity in cells; this explains why the EB1 dimerization domain, which disrupts native EB dimers, exhibits a dominant-negative effect. When microtubule dynamics is reconstituted with purified tubulin, EBs promote rather than inhibit catastrophes, suggesting that in cells EBs prevent catastrophes by counteracting other microtubule regulators. This probably occurs through their action on microtubule ends, because catastrophe suppression does not require the EB domains needed for binding to known EB partners.
  • Article
    Multivalent interactions facilitate motor-dependent protein accumulation at growing microtubule plus-ends
    (Nature Research, 2022-12-19) Maan, Renu ; Reese, Louis ; Volkov, Vladimir A. ; King, Matthew R. ; van der Sluis, Eli O. ; Anea, Nemo ; Evers, Wiel H. ; Jakobi, Arjen J. ; Dogterom, Marileen
    Growing microtubule ends organize end-tracking proteins into comets of mixed composition. Here using a reconstituted fission yeast system consisting of end-binding protein Mal3, kinesin Tea2 and cargo Tip1, we found that these proteins can be driven into liquid-phase droplets both in solution and at microtubule ends under crowding conditions. In the absence of crowding agents, cryo-electron tomography revealed that motor-dependent comets consist of disordered networks where multivalent interactions may facilitate non-stoichiometric accumulation of cargo Tip1. We found that two disordered protein regions in Mal3 are required for the formation of droplets and motor-dependent accumulation of Tip1, while autonomous Mal3 comet formation requires only one of them. Using theoretical modelling, we explore possible mechanisms by which motor activity and multivalent interactions may lead to the observed enrichment of Tip1 at microtubule ends. We conclude that microtubule ends may act as platforms where multivalent interactions condense microtubule-associated proteins into large multi-protein complexes.