QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 14, Issue 9, 3868-3875, September 2003

This Article Full Text Full Text (PDF) All Versions of this Article: E02-11-0766v1 14/9/3868    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kleijnen, M. F. Articles by Howley, P. M. Search for Related Content PubMed PubMed Citation Articles by Kleijnen, M. F. Articles by Howley, P. M.

The Ubiquitin-associated Domain of hPLIC-2 Interacts with the Proteasome

Maurits F. Kleijnen ^*, Rodolfo M. Alarcón, and Peter M. Howley 

Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115

Submitted November 26, 2002; Revised May 6, 2003; Accepted May 7, 2003
Monitoring Editor: Juan Bonifacino

The ubiquitin-like hPLIC proteins can associate with proteasomes, and hPLIC overexpression can specifically interfere with ubiquitin-mediated proteolysis (Kleijnen et al., 2000). Because the hPLIC proteins can also interact with certain E3 ubiquitin protein ligases, they may provide a link between the ubiquitination and proteasomal degradation machineries. The amino-terminal ubiquitin-like (ubl) domain is a proteasome-binding domain. Herein, we report that there is a second proteasome-binding domain in hPLIC-2: the carboxyl-terminal ubiquitin-associated (uba) domain. Coimmunoprecipitation experiments of wild-type and mutant hPLIC proteins revealed that the ubl and uba domains each contribute independently to hPLIC-2–proteasome binding. There is specificity for the interaction of the hPLIC-2 uba domain with proteasomes, because uba domains from several other proteins failed to bind proteasomes. Furthermore, the binding of uba domains to polyubiquitinated proteins does not seem to be sufficient for the proteasome binding. Finally, the uba domain is necessary for the ability of full-length hPLIC-2 to interfere with the ubiquitin-mediated proteolysis of p53. The PLIC uba domain has been reported to bind and affect the functions of proteins such as GABA_A receptor and presenilins. It is possible that the function of these proteins may be regulated or mediated through proteasomal degradation pathways.

^* Present address: Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115.

Corresponding author. E-mail address: peter_howley{at}hms.harvard.edu.

This article has been cited by other articles:

				R. S. Saliba, M. Pangalos, and S. J. Moss The Ubiquitin-like Protein Plic-1 Enhances the Membrane Insertion of GABAA Receptors by Increasing Their Stability within the Endoplasmic Reticulum J. Biol. Chem., July 4, 2008; 283(27): 18538 - 18544. [Abstract] [Full Text] [PDF]

				X. Li, V. Su, W. E. Kurata, C. Jin, and A. F. Lau A Novel Connexin43-interacting Protein, CIP75, Which Belongs to the UbL-UBA Protein Family, Regulates the Turnover of Connexin43 J. Biol. Chem., February 29, 2008; 283(9): 5748 - 5759. [Abstract] [Full Text] [PDF]

				J. Hamazaki, K. Sasaki, H. Kawahara, S.-i. Hisanaga, K. Tanaka, and S. Murata Rpn10-Mediated Degradation of Ubiquitinated Proteins Is Essential for Mouse Development Mol. Cell. Biol., October 1, 2007; 27(19): 6629 - 6638. [Abstract] [Full Text] [PDF]

				F. Shen, Q. Lin, Y. Gu, C. Childress, and W. Yang Activated Cdc42-associated Kinase 1 Is a Component of EGF Receptor Signaling Complex and Regulates EGF Receptor Degradation Mol. Biol. Cell, March 1, 2007; 18(3): 732 - 742. [Abstract] [Full Text] [PDF]

				A. V. Thomas, L. Herl, R. Spoelgen, M. Hiltunen, P. B. Jones, R. E. Tanzi, B. T. Hyman, and O. Berezovska Interaction between Presenilin 1 and Ubiquilin 1 as Detected by Fluorescence Lifetime Imaging Microscopy and a High-throughput Fluorescent Plate Reader J. Biol. Chem., September 8, 2006; 281(36): 26400 - 26407. [Abstract] [Full Text] [PDF]

				C. G. Almeida, R. H. Takahashi, and G. K. Gouras Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J. Neurosci., April 19, 2006; 26(16): 4277 - 4288. [Abstract] [Full Text] [PDF]

				H. Wang, P. J. Lim, C. Yin, M. Rieckher, B. E. Vogel, and M. J. Monteiro Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin Hum. Mol. Genet., March 15, 2006; 15(6): 1025 - 1041. [Abstract] [Full Text] [PDF]

				S. Kim, C. Kang, C. Y. Shin, S. W. Hwang, Y. D. Yang, W. S. Shim, M.-Y. Park, E. Kim, M. Kim, B.-M. Kim, et al. TRPV1 Recapitulates Native Capsaicin Receptor in Sensory Neurons in Association with Fas-Associated Factor 1 J. Neurosci., March 1, 2006; 26(9): 2403 - 2412. [Abstract] [Full Text] [PDF]

				M. B. Ficklin, S. Zhao, and G. Feng Ubiquilin-1 Regulates Nicotine-induced Up-regulation of Neuronal Nicotinic Acetylcholine Receptors J. Biol. Chem., October 7, 2005; 280(40): 34088 - 34095. [Abstract] [Full Text] [PDF]

				M. L. Seibenhener, J. R. Babu, T. Geetha, H. C. Wong, N. R. Krishna, and M. W. Wooten Sequestosome 1/p62 Is a Polyubiquitin Chain Binding Protein Involved in Ubiquitin Proteasome Degradation Mol. Cell. Biol., September 15, 2004; 24(18): 8055 - 8068. [Abstract] [Full Text] [PDF]