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From Proteopedia
The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with ADP-Mg-AlFx
Structural highlights
FunctionKIF2C_MOUSE In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (By similarity). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis (By similarity). Publication Abstract from PubMedMicrotubules (MTs) are dynamic structures that are fundamental for cell morphogenesis and motility. MT-associated motors work efficiently to perform their functions. Unlike other motile kinesins, KIF2 catalytically depolymerizes MTs from the peeled protofilament end during ATP hydrolysis. However, the detailed mechanism by which KIF2 drives processive MT depolymerization remains unknown. To elucidate the catalytic mechanism, the transitional KIF2-tubulin complex during MT depolymerization was analyzed through multiple methods, including atomic force microscopy, size-exclusion chromatography, multi-angle light scattering, small-angle X-ray scattering, analytical ultracentrifugation, and mass spectrometry. The analyses outlined the conformation in which one KIF2core domain binds tightly to two tubulin dimers in the middle pre-hydrolysis state during ATP hydrolysis, a process critical for catalytic MT depolymerization. The X-ray crystallographic structure of the KIF2core domain displays the activated conformation that sustains the large KIF2-tubulin 1:2 complex. Mechanism of Catalytic Microtubule Depolymerization via KIF2-Tubulin Transitional Conformation.,Ogawa T, Saijo S, Shimizu N, Jiang X, Hirokawa N Cell Rep. 2017 Sep 12;20(11):2626-2638. doi: 10.1016/j.celrep.2017.08.067. PMID:28903043[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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