NDLI: Ubiquitin-Independent Degradation of Antiapoptotic MCL-1▿

Content Provider	PubMed Central
Author	Stewart, Daniel P. Koss, Brian Madhavi, Bathina Perciavalle, Rhonda M. Bisanz, Kristen Opferman, Joseph T.
Copyright Year	2010
Abstract	Antiapoptotic myeloid cell leukemia 1 (MCL-1) is an essential modulator of survival during the development and maintenance of a variety of cell lineages. Its turnover, believed to be mediated by the ubiquitin-proteasome system, facilitates apoptosis induction in response to cellular stress. To investigate the contribution of ubiquitinylation in regulating murine MCL-1 turnover, we generated an MCL-1 mutant lacking the lysine residues required for ubiquitinylation (MCL-1KR). Here, we demonstrate that despite failing to be ubiquitinylated, the MCL-1KR protein is eliminated at a rate similar to that of wild-type MCL-1 under basal and stressed conditions. Moreover, the degradation of wild-type MCL-1 is not affected when ubiquitin-activating enzyme E1 activity is blocked. Likewise, both wild-type and MCL-1KR proteins are similarly degraded when expressed in primary lymphocytes. Supporting these findings, unmodified, in vitro-translated MCL-1 can be degraded in a cell-free system by the 20S proteasome. Taken together, these data demonstrate that MCL-1 degradation can occur independently of ubiquitinylation.
Related Links	http://dx.doi.org/10.1128/mcb.01266-09
Ending Page	3110
Page Count	12
Starting Page	3099
File Format	PDF
ISSN	02707306
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	12
Volume Number	30
Language	English
Publisher	American Society for Microbiology (ASM)
Publisher Date	2010-06-15
Access Restriction	Open
Rights Holder	American Society for Microbiology (ASM)
Subject Keyword	Cell Biology Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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