2005
DOI: 10.1074/jbc.m411718200
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Systematic Identification and Analysis of Mammalian Small Ubiquitin-like Modifier Substrates

Abstract: Small ubiquitin-like modifier (SUMO) regulates diverse cellular processes through its reversible, covalent attachment to target proteins. Many SUMO substrates are involved in transcription and chromatin structure. Sumoylation appears to regulate the functions of target proteins by changing their subcellular localization, increasing their stability, and/or mediating their binding to other proteins. Using an in vitro expression cloning approach, we have identified 40 human SUMO1 substrates. The spectrum of human… Show more

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Cited by 131 publications
(103 citation statements)
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“…3A). PIASy is known to autosumoylate itself to increase its activity (44,45). Thus the above results suggest that SYT and SYT-SSX1 can directly associate with the active form of PIASy.…”
Section: Molecular Mechanisms Of Increased Ncoa3 Expression Induced Bmentioning
confidence: 72%
“…3A). PIASy is known to autosumoylate itself to increase its activity (44,45). Thus the above results suggest that SYT and SYT-SSX1 can directly associate with the active form of PIASy.…”
Section: Molecular Mechanisms Of Increased Ncoa3 Expression Induced Bmentioning
confidence: 72%
“…The activation of SUMO precursors, their conjugation and their release from target proteins is mediated by a series of specific enzymes (Melchior et al, 2003). The attachment of multiple SUMO molecules to target proteins, polysumoylation, leads to the formation of chains and these multiple protein isoforms are detected as a ladder pattern by SDS-PAGE (Gocke et al, 2005). We show here that RGS-Rz proteins conjugate with SUMO-1/2/3 in synaptosomal membranes.…”
Section: Introductionmentioning
confidence: 75%
“…The machinery necessary for protein sumoylation is mostly nuclear (Melchior et al, 2003), although an increasing number of sumoylated proteins act outside the nucleus. These include cytosolic proteins such as a-catenin, SCG10, phosducin (Gocke et al, 2005;Klenk et al, 2006), and the membrane spanning or attached proteins GLUT1 and GLUT4 transporters (Giorgino et al, 2000), or the focal adhesion kinase (Kadaré et al, 2003). It is therefore possible that these proteins are subject to nucleocytoplasmic cycling that facilitates their sumoylation in the nucleus and the subsequent redistribution to the cytosol and/or cell membrane.…”
Section: Discussionmentioning
confidence: 99%
“…This modification has not yet been evaluated with regard to its role in BER. XRCC1 was also recently identified as a substrate for SUMO-modification but has not been characterized further [117]. PARP1 is most abundantly auto-modified by ADP-ribosylation and further modified by phosphorylation, SUMO and acetylation (Table III).…”
Section: Ber Scaffold Proteins and Post-translational Modificationsmentioning
confidence: 99%