3CO1

Crystal structure of microtubule binding domain of human EB3

Summary for 3CO1

• Entry DOI: 10.2210/pdb3co1/pdb
• Related: 1PA7 1WYO
• Descriptor: Microtubule-associated protein RP/EB family member 3 (2 entities in total)
• Functional Keywords: rp/eb family, ch domain, microtubule-binding, +tip protein, cell cycle, cell division, mitosis, phosphoprotein, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: Q9UPY8
• Total number of polymer chains: 1
• Total formula weight: 15402.82

Authors

De Groot, C.O.,Honnappa, S.,Steinmetz, M.O. (deposition date: 2008-03-27, release date: 2009-03-17, Last modification date: 2023-11-01)

Primary citation

Komarova, Y.,De Groot, C.O.,Grigoriev, I.,Gouveia, S.M.,Munteanu, E.L.,Schober, J.M.,Honnappa, S.,Buey, R.M.,Hoogenraad, C.C.,Dogterom, M.,Borisy, G.G.,Steinmetz, M.O.,Akhmanova, A.
Mammalian end binding proteins control persistent microtubule growth.
J.Cell Biol., 2009

PubMed Abstract: 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.

PubMed: 19255245
DOI: 10.1083/jcb.200807179

Experimental method

X-RAY DIFFRACTION (1.4 Å)