Ku70 is stabilized by increased cellular SUMO.
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.
Department of Pathology, Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Vyacheslav
V
Yurchenko
Zhu
Z
Xue
Vivian
V
Gama
Shigemi
S
Matsuyama
Moshe J
MJ
Sadofsky
D000818:Animals; D034961:Antigens, Nuclear / Q000378:metabolism*; D016466:CHO Cells; D006224:Cricetinae; D003412:Cricetulus; D004268:DNA-Binding Proteins / Q000378:metabolism*; D000072200:Ku Autoantigen; D015398:Signal Transduction / Q000502:physiology*; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*
D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; D000072200:Ku Autoantigen