| First Author | Xing B | Year | 2013 |
| Journal | J Biol Chem | Volume | 288 |
| Issue | 46 | Pages | 32827-36 |
| PubMed ID | 24092753 | Mgi Jnum | J:204985 |
| Mgi Id | MGI:5543844 | Doi | 10.1074/jbc.M113.489427 |
| Citation | Xing B, et al. (2013) Atypical protein kinase Clambda is critical for growth factor receptor-induced dorsal ruffle turnover and cell migration. J Biol Chem 288(46):32827-36 |
| abstractText | Galpha13, a member of the heterotrimeric G proteins, is critical for actin cytoskeletal reorganization and cell migration. Previously we have shown that Galpha13 is essential for both G protein-coupled receptor and receptor tyrosine kinase-induced actin cytoskeletal reorganization such as dynamic dorsal ruffle turnover and cell migration. Ric-8A, a non-receptor guanine nucleotide exchange factor for some heterotrimeric G proteins, is critical for coupling receptor tyrosine kinases to Galpha13. Here, we show that PDGF can induce phosphorylation of Ric-8A. Atypical protein kinase Clambda (aPKClambda) is required for Ric-8A phosphorylation. Furthermore, aPKClambda is required for PDGF-induced dorsal ruffle turnover and cell migration as demonstrated by both down-regulation of aPKClambda protein levels in cells by RNA interference and by studies in aPKClambda knock-out cells. Moreover, phosphorylation of Ric-8A modulates its subcellular localization. Hence, aPKClambda is critical for PDGF-induced actin cytoskeletal reorganization and cell migration. |
