| First Author | Saha S | Year | 2016 |
| Journal | FEBS Lett | Volume | 590 |
| Issue | 23 | Pages | 4223-4232 |
| PubMed ID | 27714782 | Mgi Jnum | J:238632 |
| Mgi Id | MGI:5823297 | Doi | 10.1002/1873-3468.12446 |
| Citation | Saha S, et al. (2016) N-terminal polar amino acids of the C2 insert of nonmuscle myosin II-C2 regulate its functional properties. FEBS Lett 590(23):4223-4232 |
| abstractText | In this study, we investigated the regions in the alternatively spliced C2 insert of nonmuscle myosin (NM) II-C conferring unique functional properties to the protein. We used constructs carrying deletions within different regions of C2 in neuronal cells; namely, the polar N terminus, the proline/serine-rich middle, and the nonpolar C terminus. We compared the wild-type NM II-C2 and deletion mutants with respect to ATPase activity, coassembly with NM II-B, regulation by myosin light-chain kinase (MLCK), and solubility, to determine the C2 region(s) involved in these processes. In addition, we examined the ability of the mutants to rescue the neurite-shortening phenotype upon NM II-C2 knockdown in Neuro-2a cells. Our data highlight the importance of the polar N terminus in NM II-C2 function. |
