Literature DB >> 12012321

Versatile protein tag, SUMO: its enzymology and biological function.

Keun Il Kim1, Sung Hee Baek, Chin Ha Chung.   

Abstract

Small ubiquitin-related modifier (SUMO) is a member of a ubiquitin-like protein family that regulates cellular function of a variety of target proteins. SUMO and ubiquitin are synthesized as precursors that need to be processed prior to conjugation to target proteins, and their mature forms have a similar tertiary structure. The mechanism for SUMO conjugation is also analogous to that of the ubiquitin system, such as the utilization of E1, E2, and E3 cascade enzymes. However, the biological consequence of SUMO modification is quite different from that of the ubiquitin system. Whereas ubiquitination of most proteins is for the degradative pathway, SUMO modification of target proteins is involved in nuclear protein targeting, formation of subnuclear structures, regulation of transcriptional activities or DNA binding abilities of transcription factors, and control of protein stability. This review will summarize the recent progress made in the enzymology of SUMO and its biological significance. Copyright 2002 Wiley-Liss, Inc.

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Year:  2002        PMID: 12012321     DOI: 10.1002/jcp.10100

Source DB:  PubMed          Journal:  J Cell Physiol        ISSN: 0021-9541            Impact factor:   6.384


  49 in total

Review 1.  Modification with SUMO. A role in transcriptional regulation.

Authors:  Alexis Verger; José Perdomo; Merlin Crossley
Journal:  EMBO Rep       Date:  2003-02       Impact factor: 8.807

2.  SUMOylation of the human cytomegalovirus 72-kilodalton IE1 protein facilitates expression of the 86-kilodalton IE2 protein and promotes viral replication.

Authors:  Michael Nevels; Wolfram Brune; Thomas Shenk
Journal:  J Virol       Date:  2004-07       Impact factor: 5.103

3.  A universal strategy for proteomic studies of SUMO and other ubiquitin-like modifiers.

Authors:  Germán Rosas-Acosta; William K Russell; Adeline Deyrieux; David H Russell; Van G Wilson
Journal:  Mol Cell Proteomics       Date:  2004-11-30       Impact factor: 5.911

4.  Ikaros SUMOylation: switching out of repression.

Authors:  Pablo Gómez-del Arco; Joseph Koipally; Katia Georgopoulos
Journal:  Mol Cell Biol       Date:  2005-04       Impact factor: 4.272

5.  Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1.

Authors:  Zheng Xu; Shannon W N Au
Journal:  Biochem J       Date:  2005-03-01       Impact factor: 3.857

6.  Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation.

Authors:  Guillaume Bossis; Cécile E Malnou; Rosa Farras; Elisabetta Andermarcher; Robert Hipskind; Manuel Rodriguez; Darja Schmidt; Stefan Muller; Isabelle Jariel-Encontre; Marc Piechaczyk
Journal:  Mol Cell Biol       Date:  2005-08       Impact factor: 4.272

7.  SUMO modification enhances p66-mediated transcriptional repression of the Mi-2/NuRD complex.

Authors:  Zihua Gong; Marc Brackertz; Rainer Renkawitz
Journal:  Mol Cell Biol       Date:  2006-06       Impact factor: 4.272

8.  Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation.

Authors:  Keun Il Kim; Nadia V Giannakopoulos; Herbert W Virgin; Dong-Er Zhang
Journal:  Mol Cell Biol       Date:  2004-11       Impact factor: 4.272

9.  SUMOylation of hnRNP-K is required for p53-mediated cell-cycle arrest in response to DNA damage.

Authors:  Seong Won Lee; Moon Hee Lee; Jong Ho Park; Sung Hwan Kang; Hee Min Yoo; Seung Hyun Ka; Young Mi Oh; Young Joo Jeon; Chin Ha Chung
Journal:  EMBO J       Date:  2012-10-23       Impact factor: 11.598

10.  Comparison of TFII-I gene family members deleted in Williams-Beuren syndrome.

Authors:  Timothy A Hinsley; Pamela Cunliffe; Hannah J Tipney; Andrew Brass; May Tassabehji
Journal:  Protein Sci       Date:  2004-10       Impact factor: 6.725

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