Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 28 July 2000:
Vol. 289. no. 5479, pp. 563 - 564
DOI: 10.1126/science.289.5479.563

Perspectives

BIOCHEMISTRY:
All in the Ubiquitin Family

Mark Hochstrasser

The job of a protein can be altered by addition of molecules such as ubiquitin or the related ubiquitin-like modifiers, which bring about changes in the protein's localization, conformation, or its interactions with other proteins. In a comprehensive Perspective, Hochstrasser brings us up to date with the many new members of the ubiquitin modifier family and their multitudinous and diverse protein targets.


The author is at Yale University, Department of Molecular Biophysics and Biochemistry, 266 Whitney Avenue, New Haven, CT 06520, USA. E-mail: mark.hochstrasser{at}yale.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
C-Terminal Modification Is Required for GABARAP-Mediated GABAA Receptor Trafficking.
Z.-W. Chen, C.-S. S. Chang, T. A. Leil, and R. W. Olsen (2007)
J. Neurosci. 27, 6655-6663
   Abstract »    Full Text »    PDF »
Phosphatidylserine in Addition to Phosphatidylethanolamine Is an in Vitro Target of the Mammalian Atg8 Modifiers, LC3, GABARAP, and GATE-16.
Y.-s. Sou, I. Tanida, M. Komatsu, T. Ueno, and E. Kominami (2006)
J. Biol. Chem. 281, 3017-3024
   Abstract »    Full Text »    PDF »
SIZ1/SIZ2 Control of Chromosome Transmission Fidelity Is Mediated by the Sumoylation of Topoisomerase II.
Y. Takahashi, V. Yong-Gonzalez, Y. Kikuchi, and A. Strunnikov (2006)
Genetics 172, 783-794
   Abstract »    Full Text »    PDF »
A Method of Mapping Protein Sumoylation Sites by Mass Spectrometry Using a Modified Small Ubiquitin-like Modifier 1 (SUMO-1) and a Computational Program.
M. Knuesel, H. T. Cheung, M. Hamady, K. K. B. Barthel, and X. Liu (2005)
Mol. Cell. Proteomics 4, 1626-1636
   Abstract »    Full Text »    PDF »
Sumoylation of MITF and Its Related Family Members TFE3 and TFEB.
A. J. Miller, C. Levy, I. J. Davis, E. Razin, and D. E. Fisher (2005)
J. Biol. Chem. 280, 146-155
   Abstract »    Full Text »    PDF »
Genetic Variation in BEACON Influences Quantitative Variation in Metabolic Syndrome-Related Phenotypes.
J. B. Jowett, K. S. Elliott, J. E. Curran, N. Hunt, K. R. Walder, G. R. Collier, P. Z. Zimmet, and J. Blangero (2004)
Diabetes 53, 2467-2472
   Abstract »    Full Text »    PDF »
High-throughput Immunoblotting. UBIQUITIN-LIKE PROTEIN ISG15 MODIFIES KEY REGULATORS OF SIGNAL TRANSDUCTION.
M. P. Malakhov, K. I. Kim, O. A. Malakhova, B. S. Jacobs, E. C. Borden, and D.-E. Zhang (2003)
J. Biol. Chem. 278, 16608-16613
   Abstract »    Full Text »    PDF »
Multiple Splice Variants of the Human HIF-3alpha Locus Are Targets of the von Hippel-Lindau E3 Ubiquitin Ligase Complex.
M. A. Maynard, H. Qi, J. Chung, E. H. L. Lee, Y. Kondo, S. Hara, R. C. Conaway, J. W. Conaway, and M. Ohh (2003)
J. Biol. Chem. 278, 11032-11040
   Abstract »    Full Text »    PDF »
Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding.
R. Kitahara and K. Akasaka (2003)
PNAS 100, 3167-3172
   Abstract »    Full Text »    PDF »
Insulin Induces Heterologous Desensitization of G Protein-Coupled Receptor and Insulin-Like Growth Factor I Signaling by Downregulating {beta}-Arrestin-1.
S. Dalle, T. Imamura, D. W. Rose, D. S. Worrall, S. Ugi, C. J. Hupfeld, and J. M. Olefsky (2002)
Mol. Cell. Biol. 22, 6272-6285
   Abstract »    Full Text »    PDF »
Lysine residues of Epstein-Barr virus-encoded nuclear antigen 2 do not confer secondary modifications via ubiquitin or SUMO-like proteins but modulate transcriptional activation.
A. Hille, A. Badu-Antwi, D. Holzer, and F. A. Grasser (2002)
J. Gen. Virol. 83, 1037-1042
   Abstract »    Full Text »    PDF »
UBP43 (USP18) Specifically Removes ISG15 from Conjugated Proteins.
M. P. Malakhov, O. A. Malakhova, K. I. Kim, K. J. Ritchie, and D.-E. Zhang (2002)
J. Biol. Chem. 277, 9976-9981
   Abstract »    Full Text »    PDF »
Cytoskeletal Regulation by the Nedd8 Ubiquitin-Like Protein Modification Pathway.
T. Kurz, L. Pintard, J. H. Willis, D. R. Hamill, P. Gonczy, M. Peter, and B. Bowerman (2002)
Science 295, 1294-1298
   Abstract »    Full Text »    PDF »
Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome.
G. CAGNEY, P. UETZ, and S. FIELDS (2001)
Physiol Genomics 7, 27-34
   Abstract »    Full Text »    PDF »
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: Identification of an acyldisulfide-linked protein-protein conjugate that is functionally analogous to the ubiquitin/E1 complex.
J. Xi, Y. Ge, C. Kinsland, F. W. McLafferty, and T. P. Begley (2001)
PNAS
   Abstract »    Full Text »    PDF »
A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control.
L. Li, J. Liao, J. Ruland, T. W. Mak, and S. N. Cohen (2001)
PNAS 98, 1619-1624
   Abstract »    Full Text »    PDF »
UBP43 (USP18) Specifically Removes ISG15 from Conjugated Proteins.
M. P. Malakhov, O. A. Malakhova, K. I. Kim, K. J. Ritchie, and D.-E. Zhang (2002)
J. Biol. Chem. 277, 9976-9981
   Abstract »    Full Text »    PDF »
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: Identification of an acyldisulfide-linked protein-protein conjugate that is functionally analogous to the ubiquitin/E1 complex.
J. Xi, Y. Ge, C. Kinsland, F. W. McLafferty, and T. P. Begley (2001)
PNAS 98, 8513-8518
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)