Proteasomal ATPase-Associated Factor 1 Negatively Regulates Proteasome Activity by Interacting with Proteasomal ATPases

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Published in:	Molecular and Cellular Biology Vol. 25; no. 9; pp. 3842 - 3853
Main Authors:	Park, Yoon, Hwang, Yong-Pil, Lee, Jong-Sik, Seo, Sang-Hyun, Yoon, Sungjoo Kim, Yoon, Jong-Bok
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 01-05-2005 Taylor & Francis
Subjects:	Adaptor Proteins, Signal Transducing Adenosine Triphosphatases - antagonists & inhibitors Adenosine Triphosphatases - metabolism Amino Acid Sequence Carrier Proteins - genetics Carrier Proteins - physiology Down-Regulation Endopeptidases - metabolism HeLa Cells Humans Molecular Sequence Data Proteasome Endopeptidase Complex - metabolism Proteasome Inhibitors Sequence Alignment Signal Transduction Transcriptional Activation
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Abstract	Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB
AbstractList	The 26S proteasome, composed of the 20S core and the 19S regulatory complex, plays a central role in ubiquitin-dependent proteolysis by catalyzing degradation of polyubiquitinated proteins. In a search for proteins involved in regulation of the proteasome, we affinity purified the 19S regulatory complex from HeLa cells and identified a novel protein of 43 kDa in size as an associated protein. Immunoprecipitation analyses suggested that this protein specifically interacted with the proteasomal ATPases. Hence the protein was named proteasomal ATPase-associated factor 1 (PAAF1). Immunoaffinity purification of PAAF1 confirmed its interaction with the 19S regulatory complex and further showed that the 19S regulatory complex bound with PAAF1 was not stably associated with the 20S core. Overexpression of PAAF1 in HeLa cells decreased the level of the 20S core associated with the 19S complex in a dose-dependent fashion, suggesting that PAAF1 binding to proteasomal ATPases inhibited the assembly of the 26S proteasome. Proteasomal degradation assays using reporters based on green fluorescent protein revealed that overexpression of PAAF1 inhibited the proteasome activity in vivo. Furthermore, the suppression of PAAF1 expression that is mediated by small inhibitory RNA enhanced the proteasome activity. These results suggest that PAAF1 functions as a negative regulator of the proteasome by controlling the assembly/disassembly of the proteasome. Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB
Author	Jong-Bok Yoon Sang-Hyun Seo Yoon Park Yong-Pil Hwang Jong-Sik Lee Sungjoo Kim Yoon
AuthorAffiliation	Department of Biochemistry and Protein Network Research Center, Yonsei University, Seoul 120-749, Korea, 1 Department of Biomedical Sciences, Catholic University of Korea, Seoul 137-040, Korea 2
AuthorAffiliation_xml	– name: Department of Biochemistry and Protein Network Research Center, Yonsei University, Seoul 120-749, Korea, 1 Department of Biomedical Sciences, Catholic University of Korea, Seoul 137-040, Korea 2
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BackLink	https://www.ncbi.nlm.nih.gov/pubmed/15831487$$D View this record in MEDLINE/PubMed
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Corresponding author. Mailing address: Department of Biochemistry, College of Science, Yonsei University, 134 Shinchon-Dong, Seodaemoon-Gu, Seoul 120-749, Korea. Phone: 82-2-2123-2704. Fax: 82-2-392-3488. E-mail: yoonj@yonsei.ac.kr. These two authors contributed equally to this work.
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Snippet	Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... The 26S proteasome, composed of the 20S core and the 19S regulatory complex, plays a central role in ubiquitin-dependent proteolysis by catalyzing degradation...
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SubjectTerms	Adaptor Proteins, Signal Transducing Adenosine Triphosphatases - antagonists & inhibitors Adenosine Triphosphatases - metabolism Amino Acid Sequence Carrier Proteins - genetics Carrier Proteins - physiology Down-Regulation Endopeptidases - metabolism HeLa Cells Humans Molecular Sequence Data Proteasome Endopeptidase Complex - metabolism Proteasome Inhibitors Sequence Alignment Signal Transduction Transcriptional Activation
Title	Proteasomal ATPase-Associated Factor 1 Negatively Regulates Proteasome Activity by Interacting with Proteasomal ATPases
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