Sumoylation regulates diverse biological processes.

@article{citeulike:2900979, abstract = {Ten years after its discovery, the small ubiquitin-like protein modifier (SUMO) has emerged as a key regulator of proteins. While early studies indicated that sumoylation takes place mainly in the nucleus, an increasing number of non-nuclear substrates have recently been identified, suggesting a wider stage for sumoylation in the cell. Unlike ubiquitylation, which primarily targets a substrate for degradation, sumoylation regulates a substrate's functions mainly by altering the intracellular localization, protein-protein interactions or other types of post-translational modifications. These changes in turn affect gene expression, genomic and chromosomal stability and integrity, and signal transduction. Sumoylation is counter-balanced by desumoylation, and well-balanced sumoylation is essential for normal cellular behaviors. Loss of the balance has been associated with a number of diseases. This paper reviews recent progress in the study of SUMO pathways, substrates, and cellular functions and highlights important findings that have accelerated advances in this study field and link sumoylation to human diseases.}, address = {Center for Cell Biology and Cancer Research, Albany Medical College, 47 New Scotland Avenue, MC-165, Albany, New York 12208, USA. zhaojh@mail.amc.edu}, author = {Zhao, J. }, citeulike-article-id = {2900979}, doi = {http://dx.doi.org/10.1007/s00018-007-7137-4}, issn = {1420-682X}, journal = {Cellular and molecular life sciences : CMLS}, keywords = {sumo}, month = {December}, number = {23}, pages = {3017--3033}, posted-at = {2008-06-17 04:30:56}, priority = {2}, title = {Sumoylation regulates diverse biological processes.}, url = {http://dx.doi.org/10.1007/s00018-007-7137-4}, volume = {64}, year = {2007} }

TY - JOUR ID - citeulike:2900979 L3 - citeulike-article-id:2900979 TI - Sumoylation regulates diverse biological processes. JF - Cellular and molecular life sciences : CMLS VL - 64 IS - 23 SP - 3017 EP - 3033 AD - Center for Cell Biology and Cancer Research, Albany Medical College, 47 New Scotland Avenue, MC-165, Albany, New York 12208, USA. zhaojh@mail.amc.edu SN - 1420-682X N2 - Ten years after its discovery, the small ubiquitin-like protein modifier (SUMO) has emerged as a key regulator of proteins. While early studies indicated that sumoylation takes place mainly in the nucleus, an increasing number of non-nuclear substrates have recently been identified, suggesting a wider stage for sumoylation in the cell. Unlike ubiquitylation, which primarily targets a substrate for degradation, sumoylation regulates a substrate's functions mainly by altering the intracellular localization, protein-protein interactions or other types of post-translational modifications. These changes in turn affect gene expression, genomic and chromosomal stability and integrity, and signal transduction. Sumoylation is counter-balanced by desumoylation, and well-balanced sumoylation is essential for normal cellular behaviors. Loss of the balance has been associated with a number of diseases. This paper reviews recent progress in the study of SUMO pathways, substrates, and cellular functions and highlights important findings that have accelerated advances in this study field and link sumoylation to human diseases. KW - sumo AU - Zhao, J PY - 2007/12// UR - http://dx.doi.org/10.1007/s00018-007-7137-4 ER -