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SUMO Regulation of Cellular Processes by Van G. Wilson (auth.), Van G. Wilson (eds.)

By Van G. Wilson (auth.), Van G. Wilson (eds.)

Over a decade in the past, a small mobile protein of 12 kDa, with 18% homology to the well known ubiquitin protein, used to be co-discovered and termed Small Ubiquitin-like Modifier, or SUMO. Sumoylation is a post-translational amendment that makes use of SUMO because the modifier staff covalently hooked up to focus on substrates. This state-of-the artwork assessment at the sumoylation process bargains with protein amendment because it relates to legislation of numerous mobile features. each one bankruptcy has been written by way of a number one researcher and covers the position of sumoylation in basic biochemical actions (transcription, RNA processing, chromatin remodelling, DNA fix, nucleocytoplasmic shipping, ion channel rules, and metabolic pathways). The textual content additionally examines the half sumoylation performs in severe mobile tactics reminiscent of mitosis, meiosis, differentiation, senescence, and apoptosis. finally, the rising position of sumoylation in particular illnesses, together with melanoma and diabetes in addition to neurodegenerative ones, is explored with an emphasis on defining molecular mechanisms which may offer new pursuits for therapy or prevention. whereas SUMO was once found greater than 10 years in the past, this can be nonetheless a comparatively younger box, and lots more and plenty continues to be found in regards to the biochemical and organic homes of this transformation method. in precisely the previous couple of years, it has turn into transparent that sumoylation modifies countless numbers of mobile proteins, and there was elevated appreciation for the breadth of mobile capabilities which are impacted through this post-translational amendment.

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EMBO J. 25, 5317–5328. Mabb, A. , Wuerzberger-Davis, S. M. , 2006, PIASy mediates NEMO sumoylation and nf-kappab activation in response to genotoxic stress. Nat. Cell Biol. 8, 986–993. Mascle, X. , Estephan, P. , 2007, Sumoylation of the transcriptional intermediary factor 1beta (tif1beta), the co-repressor of the krab multifinger 2 SUMO Modification and Transcriptional Regulation 39 proteins, is required for its transcriptional activity and is modulated by the krab domain. J. Biol. Chem. 282, 10190–10202.

Nalbant, D. and Williams, S. , 1999, A short conserved motif is required for repressor domain function in the myeloid-specific transcription factor CCAAT/enhancerbinding protein epsilon. J. Biol. Chem. 274, 4147–4154. , Prosperi, M. , Boule, C. , 2005, A kruppel zinc finger of znf 146 interacts with the sumo-1 conjugating enzyme Ubc9 and is sumoylated in vivo. Mol. Cell. Biochem. 271, 215–223. Arnosti, D. N. and Kulkarni, M. , 2005, Transcriptional enhancers: intelligent enhanceosomes or flexible billboards?

Exp. Cell Res. 314, 1585–1594. , Nguyen, H. P. and Yeh, E. , 1997, Preferential modification of nuclear proteins by a novel ubiquitin-like molecule. J. Biol. Chem. 272, 14001–14004. , Nakayama, K. , Kikuchi, A. , 2004, Small ubiquitinlike modifier 1 (SUMO-1) modification of the synergy control motif of ad4 binding protein/steroidogenic factor 1 (ad4bp/sf-1) regulates synergistic transcription between ad4bp/sf-1 and sox9. Mol. Endocrinol. 18, 2451–2462. , Janne, O. A. and Palvimo, J. , 2002, The nuclear receptor interaction domain of grip1 is modulated by covalent attachment of SUMO-1.

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