| First Author | Alvarez B | Year | 2008 |
| Journal | J Cell Physiol | Volume | 214 |
| Issue | 2 | Pages | 474-82 |
| PubMed ID | 17654484 | Mgi Jnum | J:196103 |
| Mgi Id | MGI:5486551 | Doi | 10.1002/jcp.21215 |
| Citation | Alvarez B, et al. (2008) Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes migration of myoblasts and affects focal adhesions. J Cell Physiol 214(2):474-82 |
| abstractText | Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) binds specifically to the beta1 integrin subunit cytoplasmic domain. We observed that RNAi-induced knockdown of ICAP-1 reduced migration of C2C12 myoblasts on the beta1 integrin ligand laminin and that overexpression of ICAP-1 increased this migration. In contrast, migration on the beta3 integrin ligand vitronectin was not affected. ICAP-1 knockdown also greatly diminished migration of microvascular endothelial cells on collagen. The number of central focal adhesions in C2C12 cells on laminin was reduced by ICAP-1 knockdown and increased by ICAP-1 overexpression. Previously, we demonstrated that ICAP-1 binds to the ROCK-I kinase and translocates ROCK-I to the plasma membrane. We show here that the ROCK kinase inhibitor Y27362 reduces migration on laminin and causes a loss of central focal adhesions, similarly as ICAP-1 knockdown. ICAP-1 and ROCK were co-immune-precipitated from C2C12 cells, and in cells that overexpressed ICAP-1, YFP-ROCK was translocated to membrane ruffles. These results indicate that ICAP-1 regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. This is likely due to ICAP-1-induced translocation of ROCK to beta1 integrin attachment sites. |
