Ku70 is stabilized by increased cellular SUMO

Vyacheslav Yurchenko, Zhu Xue, Vivian Gama, Shigemi Matsuyama, Moshe J. Sadofsky

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Ku70 is a protein that finds itself at the heart of several important cellular processes. It is essential to the non-homologous end joining pathway as a part of the DNA-end binding complex, required for proper maintenance of telomeres and contributes to DNA damage recognition and regulation of apoptosis. Forces that regulate Ku70 are therefore likely to have large consequences on the physiologic state of the cell. We report here that transient expression of the small protein SUMO resulted in a dramatic increase in the abundance of Ku70. Surprisingly, the direct SUMOylation of Ku70 does not appear to be required for this effect. Rather, Ku70 appears to be stabilized through indirect effects on the rate of degradation. The same outcome was obtained by raising the expression of enzymes that promote SUMOylation. It is likely that many other proteins will be similarly regulated, providing a general control of cellular state.

Original languageEnglish (US)
Pages (from-to)263-268
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume366
Issue number1
DOIs
StatePublished - Feb 1 2008

Fingerprint

Sumoylation
SUMO-1 Protein
DNA
Telomere
Joining
DNA Damage
Proteins
Maintenance
Apoptosis
Degradation
Enzymes

Keywords

  • DNA repair
  • Ku70
  • SUMO

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Ku70 is stabilized by increased cellular SUMO. / Yurchenko, Vyacheslav; Xue, Zhu; Gama, Vivian; Matsuyama, Shigemi; Sadofsky, Moshe J.

In: Biochemical and Biophysical Research Communications, Vol. 366, No. 1, 01.02.2008, p. 263-268.

Research output: Contribution to journalArticle

Yurchenko, Vyacheslav ; Xue, Zhu ; Gama, Vivian ; Matsuyama, Shigemi ; Sadofsky, Moshe J. / Ku70 is stabilized by increased cellular SUMO. In: Biochemical and Biophysical Research Communications. 2008 ; Vol. 366, No. 1. pp. 263-268.
@article{482bbbbbedbc4567ba6430ceda6ca5fd,
title = "Ku70 is stabilized by increased cellular SUMO",
abstract = "Ku70 is a protein that finds itself at the heart of several important cellular processes. It is essential to the non-homologous end joining pathway as a part of the DNA-end binding complex, required for proper maintenance of telomeres and contributes to DNA damage recognition and regulation of apoptosis. Forces that regulate Ku70 are therefore likely to have large consequences on the physiologic state of the cell. We report here that transient expression of the small protein SUMO resulted in a dramatic increase in the abundance of Ku70. Surprisingly, the direct SUMOylation of Ku70 does not appear to be required for this effect. Rather, Ku70 appears to be stabilized through indirect effects on the rate of degradation. The same outcome was obtained by raising the expression of enzymes that promote SUMOylation. It is likely that many other proteins will be similarly regulated, providing a general control of cellular state.",
keywords = "DNA repair, Ku70, SUMO",
author = "Vyacheslav Yurchenko and Zhu Xue and Vivian Gama and Shigemi Matsuyama and Sadofsky, {Moshe J.}",
year = "2008",
month = "2",
day = "1",
doi = "10.1016/j.bbrc.2007.11.136",
language = "English (US)",
volume = "366",
pages = "263--268",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Ku70 is stabilized by increased cellular SUMO

AU - Yurchenko, Vyacheslav

AU - Xue, Zhu

AU - Gama, Vivian

AU - Matsuyama, Shigemi

AU - Sadofsky, Moshe J.

PY - 2008/2/1

Y1 - 2008/2/1

N2 - Ku70 is a protein that finds itself at the heart of several important cellular processes. It is essential to the non-homologous end joining pathway as a part of the DNA-end binding complex, required for proper maintenance of telomeres and contributes to DNA damage recognition and regulation of apoptosis. Forces that regulate Ku70 are therefore likely to have large consequences on the physiologic state of the cell. We report here that transient expression of the small protein SUMO resulted in a dramatic increase in the abundance of Ku70. Surprisingly, the direct SUMOylation of Ku70 does not appear to be required for this effect. Rather, Ku70 appears to be stabilized through indirect effects on the rate of degradation. The same outcome was obtained by raising the expression of enzymes that promote SUMOylation. It is likely that many other proteins will be similarly regulated, providing a general control of cellular state.

AB - Ku70 is a protein that finds itself at the heart of several important cellular processes. It is essential to the non-homologous end joining pathway as a part of the DNA-end binding complex, required for proper maintenance of telomeres and contributes to DNA damage recognition and regulation of apoptosis. Forces that regulate Ku70 are therefore likely to have large consequences on the physiologic state of the cell. We report here that transient expression of the small protein SUMO resulted in a dramatic increase in the abundance of Ku70. Surprisingly, the direct SUMOylation of Ku70 does not appear to be required for this effect. Rather, Ku70 appears to be stabilized through indirect effects on the rate of degradation. The same outcome was obtained by raising the expression of enzymes that promote SUMOylation. It is likely that many other proteins will be similarly regulated, providing a general control of cellular state.

KW - DNA repair

KW - Ku70

KW - SUMO

UR - http://www.scopus.com/inward/record.url?scp=37549063048&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=37549063048&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2007.11.136

DO - 10.1016/j.bbrc.2007.11.136

M3 - Article

C2 - 18062920

AN - SCOPUS:37549063048

VL - 366

SP - 263

EP - 268

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -