Crosstalk between NDR kinase pathways coordinates cell cycle dependent actin rearrangements
dc.contributor.author | Gupta, Sneha | |
dc.contributor.author | McCollum, Dannel | |
dc.date | 2022-08-11T08:09:40.000 | |
dc.date.accessioned | 2022-08-23T16:39:22Z | |
dc.date.available | 2022-08-23T16:39:22Z | |
dc.date.issued | 2011-11-11 | |
dc.date.submitted | 2012-03-22 | |
dc.identifier.citation | Cell Div. 2011 Nov 11;6:19. <a href="http://dx.doi.org/10.1186/1747-1028-6-19" target="_blank">Link to article on publisher's site</a> | |
dc.identifier.issn | 1747-1028 (Linking) | |
dc.identifier.doi | 10.1186/1747-1028-6-19 | |
dc.identifier.pmid | 22079013 | |
dc.identifier.pmid | 22079013 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/39457 | |
dc.description | <p>First author Sneha Gupta is a doctoral student in the Interdisciplinary Graduate Program in the Graduate School of Biomedical Sciences (GSBS) at UMass Medical School.</p> | |
dc.description.abstract | Regulation of cytoskeletal remodeling is essential for cell cycle transitions. In fission yeast two NDR kinase signaling cascades, MOR and SIN, regulate the actin cytoskeleton to promote polarized growth during interphase and cytokinesis respectively. Our understanding of how these signaling pathways are coordinated to assist transition between the two cell-cycle stages is limited. Here, we review work from our laboratory, which reveals that cross talk between the SIN and MOR pathways is required for inhibition of interphase polarity programs during cytokinesis. Given the conservation of NDR kinase signaling pathways, our results may define general mechanisms by which these pathways are coordinated in higher organisms. | |
dc.language.iso | en_US | |
dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=22079013&dopt=Abstract">Link to Article in PubMed</a> | |
dc.relation.url | http://dx.doi.org/10.1186/1747-1028-6-19 | |
dc.rights | © 2011 Gupta and McCollum; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<a href="http://creativecommons.org/licenses/by/2.0">http://creativecommons.org/licenses/by/2.0</a>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. | |
dc.subject | Cell Cycle Checkpoints | |
dc.subject | Cytokinesis | |
dc.subject | Actin Cytoskeleton | |
dc.subject | Protein-Serine-Threonine Kinases | |
dc.subject | Cell Polarity | |
dc.subject | Cell Biology | |
dc.subject | Cellular and Molecular Physiology | |
dc.title | Crosstalk between NDR kinase pathways coordinates cell cycle dependent actin rearrangements | |
dc.type | Journal Article | |
dc.source.journaltitle | Cell division | |
dc.source.volume | 6 | |
dc.identifier.legacyfulltext | https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=3252&context=oapubs&unstamped=1 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/oapubs/2253 | |
dc.identifier.contextkey | 2691089 | |
refterms.dateFOA | 2022-08-23T16:39:22Z | |
html.description.abstract | <p>Regulation of cytoskeletal remodeling is essential for cell cycle transitions. In fission yeast two NDR kinase signaling cascades, MOR and SIN, regulate the actin cytoskeleton to promote polarized growth during interphase and cytokinesis respectively. Our understanding of how these signaling pathways are coordinated to assist transition between the two cell-cycle stages is limited. Here, we review work from our laboratory, which reveals that cross talk between the SIN and MOR pathways is required for inhibition of interphase polarity programs during cytokinesis. Given the conservation of NDR kinase signaling pathways, our results may define general mechanisms by which these pathways are coordinated in higher organisms.</p> | |
dc.identifier.submissionpath | oapubs/2253 | |
dc.contributor.department | Program in Cell Dynamics | |
dc.contributor.department | Department of Microbiology and Physiological Systems | |
dc.source.pages | 19 |