Protein modification by SUMO. Export

@article{citeulike:1276523, abstract = {Small ubiquitin-related modifier (SUMO) family proteins function by becoming covalently attached to other proteins as post-translational modifications. SUMO modifies many proteins that participate in diverse cellular processes, including transcriptional regulation, nuclear transport, maintenance of genome integrity, and signal transduction. Reversible attachment of SUMO is controlled by an enzyme pathway that is analogous to the ubiquitin pathway. The functional consequences of SUMO attachment vary greatly from substrate to substrate, and in many cases are not understood at the molecular level. Frequently SUMO alters interactions of substrates with other proteins or with DNA, but SUMO can also act by blocking ubiquitin attachment sites. An unusual feature of SUMO modification is that, for most substrates, only a small fraction of the substrate is sumoylated at any given time. This review discusses our current understanding of how SUMO conjugation is controlled, as well as the roles of SUMO in a number of biological processes.}, address = {Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. erica.johnson@jefferson.edu}, author = {Johnson, E. S.}, citeulike-article-id = {1276523}, citeulike-linkout-0 = {http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biochem.73.011303.074118}, citeulike-linkout-1 = {http://dx.doi.org/10.1146/annurev.biochem.73.011303.074118}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/15189146}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=15189146}, doi = {10.1146/annurev.biochem.73.011303.074118}, issn = {0066-4154}, journal = {Annu Rev Biochem}, keywords = {outside, review}, pages = {355--382}, posted-at = {2007-05-04 07:24:43}, priority = {2}, title = {Protein modification by SUMO.}, url = {http://dx.doi.org/10.1146/annurev.biochem.73.011303.074118}, volume = {73}, year = {2004} }

TY - JOUR ID - citeulike:1276523 L3 - citeulike-article-id:1276523 N2 - Small ubiquitin-related modifier (SUMO) family proteins function by becoming covalently attached to other proteins as post-translational modifications. SUMO modifies many proteins that participate in diverse cellular processes, including transcriptional regulation, nuclear transport, maintenance of genome integrity, and signal transduction. Reversible attachment of SUMO is controlled by an enzyme pathway that is analogous to the ubiquitin pathway. The functional consequences of SUMO attachment vary greatly from substrate to substrate, and in many cases are not understood at the molecular level. Frequently SUMO alters interactions of substrates with other proteins or with DNA, but SUMO can also act by blocking ubiquitin attachment sites. An unusual feature of SUMO modification is that, for most substrates, only a small fraction of the substrate is sumoylated at any given time. This review discusses our current understanding of how SUMO conjugation is controlled, as well as the roles of SUMO in a number of biological processes. JF - Annu Rev Biochem SN - 0066-4154 AD - Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. erica.johnson@jefferson.edu EP - 382 TI - Protein modification by SUMO. VL - 73 SP - 355 KW - outside KW - review AU - Johnson, ES PY - 2004/// UR - http://dx.doi.org/10.1146/annurev.biochem.73.011303.074118 ER -