Cell cycle-dependent SUMO-1 conjugation to nuclear mitotic apparatus protein (NuMA)

Jae Sung Seo; Ha Na Kim; Sun Jick Kim; Jiyoung Bang; Eun A. Kim; Ki Sa Sung; Hyun Joo Yoon; Hae Yong Yoo; Cheol Yong Choi

doi:10.1016/j.bbrc.2013.11.107

Cell cycle-dependent SUMO-1 conjugation to nuclear mitotic apparatus protein (NuMA)

Jae Sung Seo, Ha Na Kim, Sun Jick Kim, Jiyoung Bang, Eun A. Kim, Ki Sa Sung, Hyun Joo Yoon, Hae Yong Yoo, Cheol Yong Choi

Department of Biological Sciences

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

9 Scopus citations

Abstract

Covalent conjugation of proteins with small ubiquitin-like modifier 1 (SUMO-1) plays a critical role in a variety of cellular functions including cell cycle control, replication, and transcriptional regulation. Nuclear mitotic apparatus protein (NuMA) localizes to spindle poles during mitosis, and is an essential component in the formation and maintenance of mitotic spindle poles. Here we show that NuMA is a target for covalent conjugation to SUMO-1. We find that the lysine 1766 residue is the primary NuMA acceptor site for SUMO-1 conjugation. Interestingly, SUMO modification of endogenous NuMA occurs at the entry into mitosis and this modification is reversed after exiting from mitosis. Knockdown of Ubc9 or forced expression of SENP1 results in impairment of the localization of NuMA to mitotic spindle poles during mitosis. The SUMOylation-deficient NuMA mutant is defective in microtubule bundling, and multiple spindles are induced during mitosis. The mitosis-dependent dynamic SUMO-1 modification of NuMA might contribute to NuMA-mediated formation and maintenance of mitotic spindle poles during mitosis.

Original language	English
Pages (from-to)	259-265
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	443
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2013.11.107
State	Published - 3 Jan 2014

Keywords

Multiple spindle poles
NuMA
SENP1
Small ubiquitin-like modifier-1

Access to Document

10.1016/j.bbrc.2013.11.107

Cite this

@article{9ac046447c9e4273a1dc5af3113c6376,

title = "Cell cycle-dependent SUMO-1 conjugation to nuclear mitotic apparatus protein (NuMA)",

abstract = "Covalent conjugation of proteins with small ubiquitin-like modifier 1 (SUMO-1) plays a critical role in a variety of cellular functions including cell cycle control, replication, and transcriptional regulation. Nuclear mitotic apparatus protein (NuMA) localizes to spindle poles during mitosis, and is an essential component in the formation and maintenance of mitotic spindle poles. Here we show that NuMA is a target for covalent conjugation to SUMO-1. We find that the lysine 1766 residue is the primary NuMA acceptor site for SUMO-1 conjugation. Interestingly, SUMO modification of endogenous NuMA occurs at the entry into mitosis and this modification is reversed after exiting from mitosis. Knockdown of Ubc9 or forced expression of SENP1 results in impairment of the localization of NuMA to mitotic spindle poles during mitosis. The SUMOylation-deficient NuMA mutant is defective in microtubule bundling, and multiple spindles are induced during mitosis. The mitosis-dependent dynamic SUMO-1 modification of NuMA might contribute to NuMA-mediated formation and maintenance of mitotic spindle poles during mitosis.",

keywords = "Multiple spindle poles, NuMA, SENP1, Small ubiquitin-like modifier-1",

author = "Seo, \{Jae Sung\} and Kim, \{Ha Na\} and Kim, \{Sun Jick\} and Jiyoung Bang and Kim, \{Eun A.\} and Sung, \{Ki Sa\} and Yoon, \{Hyun Joo\} and Yoo, \{Hae Yong\} and Choi, \{Cheol Yong\}",

year = "2014",

month = jan,

day = "3",

doi = "10.1016/j.bbrc.2013.11.107",

language = "English",

volume = "443",

pages = "259--265",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - Cell cycle-dependent SUMO-1 conjugation to nuclear mitotic apparatus protein (NuMA)

AU - Seo, Jae Sung

AU - Kim, Ha Na

AU - Kim, Sun Jick

AU - Bang, Jiyoung

AU - Kim, Eun A.

AU - Sung, Ki Sa

AU - Yoon, Hyun Joo

AU - Yoo, Hae Yong

AU - Choi, Cheol Yong

PY - 2014/1/3

Y1 - 2014/1/3

N2 - Covalent conjugation of proteins with small ubiquitin-like modifier 1 (SUMO-1) plays a critical role in a variety of cellular functions including cell cycle control, replication, and transcriptional regulation. Nuclear mitotic apparatus protein (NuMA) localizes to spindle poles during mitosis, and is an essential component in the formation and maintenance of mitotic spindle poles. Here we show that NuMA is a target for covalent conjugation to SUMO-1. We find that the lysine 1766 residue is the primary NuMA acceptor site for SUMO-1 conjugation. Interestingly, SUMO modification of endogenous NuMA occurs at the entry into mitosis and this modification is reversed after exiting from mitosis. Knockdown of Ubc9 or forced expression of SENP1 results in impairment of the localization of NuMA to mitotic spindle poles during mitosis. The SUMOylation-deficient NuMA mutant is defective in microtubule bundling, and multiple spindles are induced during mitosis. The mitosis-dependent dynamic SUMO-1 modification of NuMA might contribute to NuMA-mediated formation and maintenance of mitotic spindle poles during mitosis.

AB - Covalent conjugation of proteins with small ubiquitin-like modifier 1 (SUMO-1) plays a critical role in a variety of cellular functions including cell cycle control, replication, and transcriptional regulation. Nuclear mitotic apparatus protein (NuMA) localizes to spindle poles during mitosis, and is an essential component in the formation and maintenance of mitotic spindle poles. Here we show that NuMA is a target for covalent conjugation to SUMO-1. We find that the lysine 1766 residue is the primary NuMA acceptor site for SUMO-1 conjugation. Interestingly, SUMO modification of endogenous NuMA occurs at the entry into mitosis and this modification is reversed after exiting from mitosis. Knockdown of Ubc9 or forced expression of SENP1 results in impairment of the localization of NuMA to mitotic spindle poles during mitosis. The SUMOylation-deficient NuMA mutant is defective in microtubule bundling, and multiple spindles are induced during mitosis. The mitosis-dependent dynamic SUMO-1 modification of NuMA might contribute to NuMA-mediated formation and maintenance of mitotic spindle poles during mitosis.

KW - Multiple spindle poles

KW - NuMA

KW - SENP1

KW - Small ubiquitin-like modifier-1

UR - https://www.scopus.com/pages/publications/84890856486

U2 - 10.1016/j.bbrc.2013.11.107

DO - 10.1016/j.bbrc.2013.11.107

M3 - Article

C2 - 24309115

AN - SCOPUS:84890856486

SN - 0006-291X

VL - 443

SP - 259

EP - 265

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Cell cycle-dependent SUMO-1 conjugation to nuclear mitotic apparatus protein (NuMA)

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this