JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on August 29, 2003
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
278/35/32905    most recent
M212057200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Tanaka, T.
Right arrow Articles by Kamitani, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tanaka, T.
Right arrow Articles by Kamitani, T.
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?

Papers In Press, published online ahead of print June 19, 2003
J. Biol. Chem, 10.1074/jbc.M212057200
Submitted on November 26, 2002
Revised on June 19, 2003
Accepted on June 19, 2003

Regulation of NEDD8 conjugation system by a splicing variant, NUB1L

Tomoaki Tanaka, Hidenori Kawashima, Edward T. H. Yeh, and Tetsu Kamitani

Cardiology Dept., University of Texas M.D.Anderson Cancer Center, Houston, TX 77030

Corresponding Author: tetsu.kamitani{at}uth.tmc.edu

NEDD8 is a ubiquitin-like protein that controls vital biological events through its conjugation to target proteins. We previously identified a negative regulator of the NEDD8 conjugation system, NUB1, which works by recruiting NEDD8 and its conjugates to the proteasome for degradation. Recently, we found its splicing variant, NUB1L. It possesses an insertion of 14 amino acids that codes for a UBA domain. Structural study revealed that NUB1 has a NEDD8-binding site at the C-terminus, whereas NUB1L has an additional site at the newly generated UBA domain. Interestingly, the sequence A(X4)L(X10)L(X3)L was conserved in these NEDD8-binding sites among human and other mammals. Mutational studies revealed that at least three Leu residues in the conserved sequence are required for the binding with NEDD8. Functional study suggested that the NEDD8-binding ability at the C-terminus of NUB1 and NUB1L is mainly involved in the downregulation of NEDD8, but the NEDD8-binding ability at the UBA2 domain of NUB1L is minimally or not involved at all. The NEDD8-binding ability at the UBA2 domain might be required for an unknown function of NUB1L.


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
 IOVSHome page
J. Hidalgo-de-Quintana, R. J. Evans, M. E. Cheetham, and J. van der Spuy
The Leber Congenital Amaurosis Protein AIPL1 Functions as Part of a Chaperone Heterocomplex
Invest. Ophthalmol. Vis. Sci., July 1, 2008; 49(7): 2878 - 2887.
[Abstract] [Full Text] [PDF]

Home page
 Circ. Res.Home page
J. Herrmann, L. O. Lerman, and A. Lerman
Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation
Circ. Res., May 11, 2007; 100(9): 1276 - 1291.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
K. Tanji, T. Tanaka, F. Mori, K. Kito, H. Takahashi, K. Wakabayashi, and T. Kamitani
NUB1 Suppresses the Formation of Lewy Body-Like Inclusions by Proteasomal Degradation of Synphilin-1
Am. J. Pathol., August 1, 2006; 169(2): 553 - 565.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Schmidtke, B. Kalveram, E. Weber, P. Bochtler, S. Lukasiak, M. S. Hipp, and M. Groettrup
The UBA Domains of NUB1L Are Required for Binding but Not for Accelerated Degradation of the Ubiquitin-like Modifier FAT10
J. Biol. Chem., July 21, 2006; 281(29): 20045 - 20054.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C.-M. Hecker, M. Rabiller, K. Haglund, P. Bayer, and I. Dikic
Specification of SUMO1- and SUMO2-interacting Motifs
J. Biol. Chem., June 9, 2006; 281(23): 16117 - 16127.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
M. J. Ross, M. S. Wosnitzer, M. D. Ross, B. Granelli, G. L. Gusella, M. Husain, L. Kaufman, M. Vasievich, V. D. D'Agati, P. D. Wilson, et al.
Role of Ubiquitin-Like Protein FAT10 in Epithelial Apoptosis in Renal Disease
J. Am. Soc. Nephrol., April 1, 2006; 17(4): 996 - 1004.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. S. Hipp, B. Kalveram, S. Raasi, M. Groettrup, and G. Schmidtke
FAT10, a Ubiquitin-Independent Signal for Proteasomal Degradation
Mol. Cell. Biol., May 1, 2005; 25(9): 3483 - 3491.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. van der Spuy and M. E. Cheetham
The Leber Congenital Amaurosis Protein AIPL1 Modulates the Nuclear Translocation of NUB1 and Suppresses Inclusion Formation by NUB1 Fragments
J. Biol. Chem., November 12, 2004; 279(46): 48038 - 48047.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. S. Hipp, S. Raasi, M. Groettrup, and G. Schmidtke
NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
J. Biol. Chem., April 16, 2004; 279(16): 16503 - 16510.
[Abstract] [Full Text] [PDF]


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