期刊
MOLECULAR CELL
卷 27, 期 6, 页码 976-991出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.07.023
关键词
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资金
- NIGMS NIH HHS [R37 GM038499, R37 GM038499-19] Funding Source: Medline
- PHS HHS [38499] Funding Source: Medline
Microtubule plus end binding proteins (+TlPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus ends through a similar mechanism has not been resolved. Here, we report crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1 p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces. Functional studies, however, reveal a common property that native or artificial dimerization of tubulin binding domains (including chemically induced heterodimers of EB1 and CLIP-170) induces tubulin nucleation/assembly in vitro and, in most cases, plus end tracking in living cells. We propose that +TIPs, although diverse in structure, share a common property of multimerizing tubulin, thus acting as polymerization chaperones that aid in subunit addition to the microtubule plus end.
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