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Topic:
Rapid identification of bacterial cotton blight
IGBB Scientists:
Shien Lu
Daniel Peterson
Funding:
Cotton Incorporated, USDA, & IGBB

PTMs in Conversation: Activity and Function of Deubiquitinating Enzymes Regulated via Post-Translational Modifications
IGBB Authors:
Mariola J. EdelmannPUBLICATION YEAR:
2011IMPACT FACTOR:
4.906CITATION COUNT:
71Kessler BM, Edelmann MJ (2011) PTMs in Conversation: Activity and Function of Deubiquitinating Enzymes Regulated via Post-Translational Modifications.
Cell Biochemistry and Biophysics 60(1-2): 21-38.
DOI:
10.1007/s12013-011-9176-6EID:
2-s2.0-79955941973PMID: 21480003
DOWNLOAD PDFABSTRACTDeubiquitinating enzymes (DUBs) constitute a diverse protein family and their impact on numerous biological and pathological processes has now been widely appreciated. Many DUB functions have to be tightly controlled within the cell, and this can be achieved in several ways, such as substrate-induced conformational changes, binding to adaptor proteins, proteolytic cleavage, and post-translational modifications (PTMs). This review is focused on the role of PTMs including monoubiquitination, sumoylation, acetylation, and phosphorylation as characterized and putative regulative factors of DUB function. Although this aspect of DUB functionality has not been yet thoroughly studied, PTMs represent a versatile and reversible method of controlling the role of DUBs in biological processes. In several cases PTMs might constitute a feedback mechanism insuring proper functioning of the ubiquitin proteasome system and other DUB-related pathways.


Dr. Florencia MeyerAssociate Professor
Biochemistry, Molecular Biology, Entomology & Plant PathologyIGBB Affiliate
email(662) 325-7734
Dr. Xueyan ShanAssociate Research Professor
Biochemistry, Molecular Biology, Entomology & Plant PathologyIGBB Affiliate
email(662) 325-2640
Dr. Chuan-Yu Hsu (Shu or Sue)Senior Research Associate
GENOMICS LEAD
email(662) 325-9511
Pace 121
The IGBB is supported, in part, by the following units:
The IGBB is an HPC² member center.