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8/22/2014 11:42:00 AM | Browse: 964 | Download: 890
Publication Name World Journal of Biological Chemistry
Manuscript ID 7770
Country United States
Received
2013-11-30 14:02
Peer-Review Started
2013-12-02 10:22
To Make the First Decision
2013-12-13 13:35
Return for Revision
2013-12-17 16:42
Revised
2014-01-11 09:32
Second Decision
2014-03-14 18:21
Accepted by Journal Editor-in-Chief
Accepted by Company Editor-in-Chief
2014-03-14 18:35
Articles in Press
Publication Fee Transferred
Edit the Manuscript by Language Editor
Typeset the Manuscript
2014-05-19 12:09
Publish the Manuscript Online
2014-06-11 10:30
ISSN 1949-8454 (online)
Open Access
Copyright
Article Reprints For details, please visit: http://www.wjgnet.com/bpg/gerinfo/247
Permissions For details, please visit: http://www.wjgnet.com/bpg/gerinfo/207
Publisher Baishideng Publishing Group Inc, 7041 Koll Center Parkway, Suite 160, Pleasanton, CA 94566, USA
Website http://www.wjgnet.com
Category Biochemistry & Molecular Biology
Manuscript Type Review
Article Title Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1
Manuscript Source Invited Manuscript
All Author List Xiao-Xin Sun and Mu-Shui Dai
Funding Agency and Grant Number
Funding Agency Grant Number
NIH R00 CA127134
NCI R01 CA160474
Department of Defense W81XWH-10-1-1029 (to Dai MS)
Medical Research Foundation (MRF) of Oregon to Sun XX
Corresponding Author Mu-Shui Dai, MD, PhD, Department of Molecular and Medical Genetics, School of Medicine, and the OHSU Knight Cancer Institute, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Portland, OR 97239, United States. daim@ohsu.edu
Key Words p53; MDM2; Ubiquitination; Deubiquitinating enzymes; Otub1; Cell cycle; Apoptosis
Core Tip p53 is tightly regulated by dynamic ubiquitination and deubiquitination. A number of deubiquitinating enzymes (DUBs) have been shown to regulate p53 stability and activity by either directly deubiquitinating p53 or indirectly deubiquitinating its regulators. We recently discovered that Otub1, an OTU family DUB, stabilizes and activates p53 via distinct and non-canonical mechanism wherein it suppresses the MDM2 cognate ubiquitin-conjugating enzymes UbcH5. Here we review the current progress made towards the understanding of the Otub1 functions as a potent E2 inhibitor and the underlying mechanisms.
Publish Date 2014-06-11 10:30
Citation Sun XX, Dai MS. Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1. World J Biol Chem 2014; 5(2): 75-84
URL http://www.wjgnet.com/1949-8454/full/v5/i2/75.htm
DOI http://dx.doi.org/10.4331/wjbc.v5.i2.75
Full Article (PDF) wjbc-5-75.pdf
Full Article (Word) wjbc-5-75.doc
Manuscript File 7770-Review.docx
Answering Reviewers 7770-Answering reviewers.pdf
Copyright License Agreement 7770-Copyright assignment.pdf
Peer-review Report 7770-Peer review(s).pdf
Scientific Editor Work List 7770-Scientific editor work list.doc