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

Eun Jung Park; Shin Kyoung Hur; Han Sae Lee; Shin Ai Lee; Jongbum Kwon

doi:10.1016/j.bbrc.2011.11.069

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

Eun Jung Park, Shin Kyoung Hur, Han Sae Lee, Shin Ai Lee, Jongbum Kwon

Department of Life Science

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

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.

Original language	English
Pages (from-to)	416-420
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	416
Issue number	3-4
DOIs	https://doi.org/10.1016/j.bbrc.2011.11.069
State	Published - 16 Dec 2011

Bibliographical note

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.

Keywords

Chromatin remodeling complex
INO80
Microtubule
Spindle assembly

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

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.",

keywords = "Chromatin remodeling complex, INO80, Microtubule, Spindle assembly",

author = "Park, {Eun Jung} and Hur, {Shin Kyoung} and Lee, {Han Sae} and Lee, {Shin Ai} and Jongbum Kwon",

note = "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.",

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AU - Lee, Shin Ai

AU - Kwon, Jongbum

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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.

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

Abstract

Bibliographical note

Keywords

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