JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M213070200 on February 27, 2003

J. Biol. Chem., Vol. 278, Issue 18, 15905-15910, May 2, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/18/15905    most recent
M213070200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Min, K.-W.
Right arrow Articles by Yoon, J.-B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Min, K.-W.
Right arrow Articles by Yoon, J.-B.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

TIP120A Associates with Cullins and Modulates Ubiquitin Ligase Activity*

Kyoeng-Woo MinDagger §, Ji-Won HwangDagger §, Jong-Sik LeeDagger , Yoon ParkDagger , Taka-aki Tamura, and Jong-Bok YoonDagger ||

From the Dagger  Department of Biochemistry and Protein Network Research Center, Yonsei University, Seoul 120-749, Korea and the  Department of Biology, Faculty of Science, Chiba University, Chiba 263-8522, Japan

The cullin-containing ubiquitin-protein isopeptide ligases (E3s) play an important role in regulating the abundance of key proteins involved in cellular processes such as cell cycle and cytokine signaling. They have multisubunit modular structures in which substrate recognition and the catalysis of ubiquitination are carried out by distinct polypeptides. In a search for proteins involved in regulation of cullin-containing E3 ubiquitin ligases we immunopurified CUL4B-containing complex from HeLa cells and identified TIP120A as an associated protein by mass spectrometry. Immunoprecipitation of cullins revealed that all cullins tested specifically interacted with TIP120A. Reciprocal immunoaffinity purification of TIP120A confirmed the stable interaction of TIP120A with cullin family proteins. TIP120A formed a complex with CUL1 and Rbx1, but interfered with the binding of Skp1 and F-box proteins to CUL1. TIP120A greatly reduced the ubiquitination of phosphorylated Ikappa Balpha by SCFbeta -TrCP ubiquitin ligase. These results suggest that TIP120A functions as a negative regulator of SCF E3 ubiquitin ligases and may modulate other cullin ligases in a similar fashion.

* This work was supported in part by grants from the Korea Science and Engineering Foundation through Protein Network Research Center at Yonsei University and from the Korean Ministry of Science and Technology through 21C Frontier Project.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These two authors contributed equally to this work.

|| To whom correspondence should be addressed. Tel.: 82-2-2123-2704; Fax: 82-2-392-3488; E-mail: yoonj@yonsei.ac.kr.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
E.-H. Chew and T. Hagen
Substrate-mediated Regulation of Cullin Neddylation
J. Biol. Chem., June 8, 2007; 282(23): 17032 - 17040.
[Abstract] [Full Text] [PDF]

Home page
 ANN BOT (LOND)Home page
K. Dreher and J. Callis
Ubiquitin, Hormones and Biotic Stress in Plants
Ann. Bot., May 1, 2007; 99(5): 787 - 822.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Shiraishi, C. Zhou, T. Aoki, N. Sato, T. Chiba, K. Tanaka, S. Yoshida, Y. Nabeshima, Y.-i. Nabeshima, and T.-a. Tamura
TBP-interacting Protein 120B (TIP120B)/Cullin-associated and Neddylation-dissociated 2 (CAND2) Inhibits SCF-dependent Ubiquitination of Myogenin and Accelerates Myogenic Differentiation
J. Biol. Chem., March 23, 2007; 282(12): 9017 - 9028.
[Abstract] [Full Text] [PDF]

Home page
 CirculationHome page
H. K. Park, E.-C. Park, S. W. Bae, M. Y. Park, S. W. Kim, H. S. Yoo, M. Tudev, Y. H. Ko, Y.-H. Choi, S. Kim, et al.
Expression of Heat Shock Protein 27 in Human Atherosclerotic Plaques and Increased Plasma Level of Heat Shock Protein 27 in Patients With Acute Coronary Syndrome
Circulation, August 29, 2006; 114(9): 886 - 893.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
S.-C. Lo and M. Hannink
CAND1-Mediated Substrate Adaptor Recycling Is Required for Efficient Repression of Nrf2 by Keap1
Mol. Cell. Biol., February 15, 2006; 26(4): 1235 - 1244.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
Y. Park, Y.-P. Hwang, J.-S. Lee, S.-H. Seo, S. K. Yoon, and J.-B. Yoon
Proteasomal ATPase-Associated Factor 1 Negatively Regulates Proteasome Activity by Interacting with Proteasomal ATPases
Mol. Cell. Biol., May 1, 2005; 25(9): 3842 - 3853.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S. Feng, Y. Shen, J. A. Sullivan, V. Rubio, Y. Xiong, T.-p. Sun, and X. W. Deng
Arabidopsis CAND1, an Unmodified CUL1-Interacting Protein, Is Involved in Multiple Developmental Pathways Controlled by Ubiquitin/Proteasome-Mediated Protein Degradation
PLANT CELL, July 1, 2004; 16(7): 1870 - 1882.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
H.-w. Chuang, W. Zhang, and W. M. Gray
Arabidopsis ETA2, an Apparent Ortholog of the Human Cullin-Interacting Protein CAND1, Is Required for Auxin Responses Mediated by the SCFTIR1 Ubiquitin Ligase
PLANT CELL, July 1, 2004; 16(7): 1883 - 1897.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.