Coordination of cell growth and division by the ubiquitin-proteasome system
dc.contributor.author | Benanti, Jennifer A. | |
dc.date | 2022-08-11T08:10:15.000 | |
dc.date.accessioned | 2022-08-23T17:01:17Z | |
dc.date.available | 2022-08-23T17:01:17Z | |
dc.date.issued | 2012-04-19 | |
dc.date.submitted | 2012-05-21 | |
dc.identifier.citation | Semin Cell Dev Biol. 2012 Apr 19. [Epub ahead of print] doi 10.1016/j.semcdb.2012.04.005 | |
dc.identifier.issn | 1084-9521 (Linking) | |
dc.identifier.doi | 10.1016/j.semcdb.2012.04.005 | |
dc.identifier.pmid | 22542766 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/43976 | |
dc.description.abstract | The coupling of cellular growth and division is crucial for a cell to make an accurate copy of itself. Regulated protein degradation by the ubiquitin-proteasome system (UPS) plays an important role in the coordination of these two processes. Many ubiquitin ligases, in particular the Skp1-Cullin-F-box (SCF) family and the Anaphase-Promoting Complex (APC), couple growth and division by targeting cell cycle and metabolic regulators for degradation. However, many regulatory proteins are targeted by multiple ubiquitin ligases. As a result, we are only just beginning to understand the complexities of the proteolytic regulatory network that connects cell growth and the cell cycle. | |
dc.language.iso | en_US | |
dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=22542766&dopt=Abstract">Link to article in PubMed</a> | |
dc.relation.url | http://dx.doi.org/10.1016/j.semcdb.2012.04.005 | |
dc.subject | Ubiquitin-Protein Ligase Complexes | |
dc.subject | Ubiquitin | |
dc.subject | Cell Cycle | |
dc.subject | Proteolysis | |
dc.subject | Genetics and Genomics | |
dc.title | Coordination of cell growth and division by the ubiquitin-proteasome system | |
dc.type | Journal Article | |
dc.source.journaltitle | Seminars in cell and developmental biology | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/pgfe_pp/187 | |
dc.identifier.contextkey | 2878937 | |
html.description.abstract | <p>The coupling of cellular growth and division is crucial for a cell to make an accurate copy of itself. Regulated protein degradation by the ubiquitin-proteasome system (UPS) plays an important role in the coordination of these two processes. Many ubiquitin ligases, in particular the Skp1-Cullin-F-box (SCF) family and the Anaphase-Promoting Complex (APC), couple growth and division by targeting cell cycle and metabolic regulators for degradation. However, many regulatory proteins are targeted by multiple ubiquitin ligases. As a result, we are only just beginning to understand the complexities of the proteolytic regulatory network that connects cell growth and the cell cycle.</p> | |
dc.identifier.submissionpath | pgfe_pp/187 | |
dc.contributor.department | Program in Molecular Medicine | |
dc.contributor.department | Program in Gene Function and Expression |