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The human Ino80 binds to microtubule via the E-hook of tubulin: Implications for the role in spindle assembly

Title
The human Ino80 binds to microtubule via the E-hook of tubulin: Implications for the role in spindle assembly
Authors
Park E.-J.Hur S.-K.Lee H.-S.Lee S.-A.Kwon J.
Ewha Authors
권종범허신경
SCOPUS Author ID
권종범scopus; 허신경scopus
Issue Date
2011
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 416, no. 41337, pp. 416 - 420
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The human INO80 chromatin remodeling complex, comprising the Ino80 ATPase (hIno80) and the associated proteins such as Tip49a, has been implicated in a variety of nuclear processes other than transcription. We previously have found that hIno80 interacts with tubulin and co-localizes with the mitotic spindle and is required for spindle formation. To better understand the role of hIno80 in spindle formation, we further investigated the interaction between hIno80 and microtubule. Here, we show that the N-terminal domain, dispensable for the nucleosome remodeling activity, is important for hIno80 to interact with tubulin and co-localize with the spindle. The hIno80 N-terminal domain binds to monomeric tubulin and polymerized microtubule in vitro, and the E-hook of tubulin, involved in the polymerization of microtubule, is critical for this binding. Tip49a, which has been reported to associate with the spindle, does not bind to microtubule in vitro and dispensable for spindle formation in vivo. These results suggest that hIno80 can play a direct role in the spindle assembly independent of its chromatin remodeling activity. © 2011 Elsevier Inc..
DOI
10.1016/j.bbrc.2011.11.069
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자연과학대학 > 생명과학전공 > Journal papers
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