TY - JOUR
T1 - The human Ino80 binds to microtubule via the E-hook of tubulin
T2 - Implications for the role in spindle assembly
AU - Park, Eun Jung
AU - Hur, Shin Kyoung
AU - Lee, Han Sae
AU - Lee, Shin Ai
AU - Kwon, Jongbum
N1 - Funding Information:
We thank Dr. Kunsoo Rhee and Dr. Jungmin Lee (Seoul National University) for helping in vitro microtubule assembly, and Dr. Yungdae Yun and Dr. Dongmin Kang (EwhaWomans University) for reagent supply and helpful discussions. This work was supported by a grant from the National R&D Program for Cancer Control, Ministry for Health and Welfare, Republic of Korea (1020060). E.J.P. was supported by RP Grant 2011 of EwhaWomans University.
PY - 2011/12/16
Y1 - 2011/12/16
N2 - 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.
AB - 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.
KW - Chromatin remodeling complex
KW - INO80
KW - Microtubule
KW - Spindle assembly
UR - http://www.scopus.com/inward/record.url?scp=84855900974&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2011.11.069
DO - 10.1016/j.bbrc.2011.11.069
M3 - Article
C2 - 22133677
AN - SCOPUS:84855900974
VL - 416
SP - 416
EP - 420
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3-4
ER -