Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 284, Issue 5, Pages 2617-2627Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M804847200
Keywords
-
Categories
Funding
- Canadian Institutes of Health Research and the Canadian Breast Cancer Research Alliance [151092]
- University of Windsor
- Ontario Graduate Scholarship in Science and Technology
- Natural Science and Engineering Research Council PGD2
- Natural Science and Engineering Research Council Canada Graduate Scholarship-Masters
- Canadian Institutes of Health Research New Investigator Program
Ask authors/readers for more resources
Spy1A is a cyclin-like protein required for progression through the G(1)/S phase of the cell cycle. Elevated Spy1A protein levels have been implicated in tumorigenesis and are attributed to overriding the DNA damage response and enhancing cell proliferation. Understanding how Spy1A is produced and degraded is essential in resolving how it contributes to normal and abnormal growth processes. Herein, we demonstrate that Spy1A is degraded in a cell cycle-dependent manner during mitosis via the ubiquitin-proteasome system. We have resolved the E3 ligase and essential phosphorylation sites mediating Spy1A degradation. Furthermore, we have determined that non-degradable forms of Spy1A do not trigger cell cycle arrest but, rather, contribute to uncontrolled cell growth. Further investigation into the regulation of Spy1A may reveal novel strategies for understanding the etiology and progression of specific growth disorders.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available