Differential Regulation of Focal Adhesion Kinase and Mitogen-Activated Protein Kinase Tyrosine Phosphorylation During Insulin-Like Growth Factor-I-Mediated Cytoskeletal Reorganization
dc.contributor.author | Kim, Bhumsoo | en_US |
dc.date.accessioned | 2010-04-01T15:51:07Z | |
dc.date.available | 2010-04-01T15:51:07Z | |
dc.date.issued | 1998-09 | en_US |
dc.identifier.citation | Kim, Bhumsoo (1998). "Differential Regulation of Focal Adhesion Kinase and Mitogen-Activated Protein Kinase Tyrosine Phosphorylation During Insulin-Like Growth Factor-I-Mediated Cytoskeletal Reorganization." Journal of Neurochemistry 71(3): 1333-1336. <http://hdl.handle.net/2027.42/66347> | en_US |
dc.identifier.issn | 0022-3042 | en_US |
dc.identifier.issn | 1471-4159 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/66347 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9721762&dopt=citation | en_US |
dc.description.abstract | In SH-SY5Y human neuroblastoma cells, insulin-like growth factor (IGF)-I mediates membrane ruffling and growth cone extension. We have previously shown that IGF-I activates the tyrosine phosphorylation of focal adhesion kinase (FAK) and extracellular signal-regulated protein kinase (ERK) 2. In the current study, we examined which signaling pathway underlies IGF-I-mediated FAK phosphorylation and cytoskeletal changes and determined if an intact cytoskeleton was required for IGF-I signaling. Treatment of SH-SY5Y cells with cytochalasin D disrupted the actin cytoskeleton and prevented any morphological changes induced by IGF-I. Inhibitors of phosphatidylinositol 3-kinase (PI 3-K) blocked IGF-I-mediated changes in the actin cytoskeleton as measured by membrane ruffling. In contrast, PD98059, a selective inhibitor of ERK kinase, had no effect on IGF-I-induced membrane ruffling. In parallel with effects on the actin cytoskeleton, cytochalasin D and PI 3-K inhibitors blocked IGF-I-induced FAK tyrosine phosphorylation, whereas PD98059 had no effect. It is interesting that cytochalasin D did not block IGF-I-induced ERK2 tyrosine phosphorylation. Therefore, it is likely that FAK and ERK2 tyrosine phosphorylations are regulated by separate pathways during IGF-I signaling. Our study suggests that integrity as well as dynamic motility of the actin cytoskeleton mediated by PI 3-K is required for IGF-I-induced FAK tyrosine phosphorylation, but not for ERK2 activation. | en_US |
dc.format.extent | 581630 bytes | |
dc.format.extent | 3110 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Science Ltd | en_US |
dc.rights | Blackwell Science Inc | en_US |
dc.subject.other | Insulin-like Growth Factor I | en_US |
dc.subject.other | Actin Cytoskeleton | en_US |
dc.subject.other | Focal Adhesion Kinase | en_US |
dc.subject.other | Extracellular Signal-regulated Protein Kinase | en_US |
dc.subject.other | Phosphatidylinositol 3-kinase | en_US |
dc.title | Differential Regulation of Focal Adhesion Kinase and Mitogen-Activated Protein Kinase Tyrosine Phosphorylation During Insulin-Like Growth Factor-I-Mediated Cytoskeletal Reorganization | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Neuroscience Program and Department of Neurology, University of Michigan, Ann Arbor, Michigan, U.S.A. | en_US |
dc.identifier.pmid | 9721762 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/66347/1/j.1471-4159.1998.71031333.x.pdf | |
dc.identifier.doi | 10.1046/j.1471-4159.1998.71031333.x | en_US |
dc.identifier.source | Journal of Neurochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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