Direct regulation of microtubule dynamics by KIF17 motor and tail domains

Acharya, Bipul R., Espenel, Cedric and Kreitzer, Geri (2013) Direct regulation of microtubule dynamics by KIF17 motor and tail domains. Journal of Biological Chemistry, 288 45: 32302-32313. doi:10.1074/jbc.M113.494989

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Author Acharya, Bipul R.
Espenel, Cedric
Kreitzer, Geri
Title Direct regulation of microtubule dynamics by KIF17 motor and tail domains
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2013-11-08
Sub-type Article (original research)
DOI 10.1074/jbc.M113.494989
Open Access Status Not yet assessed
Volume 288
Issue 45
Start page 32302
End page 32313
Total pages 12
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
KIF17 is a kinesin-2 family motor that interacts with EB1 at microtubule (MT) plus-ends and contributes to MT stabilization in epithelial cells. The mechanism by which KIF17 affects MTs and how its activity is regulated are not yet known. Here, we show that EB1 and the KIF17 autoinhibitory tail domain (KIF17-Tail) interacted competitively with the KIF17 catalytic motor domain (K370). Both EB1 and KIF17-Tail decreased the K0.5MT of K370, with opposing effects on MT-stimulated ATPase activity. Importantly, K370 had independent effects on MT dynamic instability, resulting in formation of long MTs without affecting polymerization rate or total polymer mass. K370 also inhibited MT depolymerization induced by dilution in vitro and by nocodazole in cells, suggesting that it acts by protecting MTplus-ends. Interestingly, KIF17-Tail bound MTs and tubulin dimers, delaying initial MT polymerization in vitro andMTregrowth in cells. However, neither EB1 nor KIF17-Tail affected K370-mediatedMTpolymerization or stabilization significantly in vitro, and EB1 was dispensable forMTstabilization by K370 in cells. Thus, although EB1 and KIF17-Tail may coordinate KIF17 catalytic activity, our data reveal a novel and direct role for KIF17 in regulating MT dynamics.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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