| First Author | Pauls SD | Year | 2020 |
| Journal | Biochem Biophys Res Commun | Volume | 527 |
| Issue | 1 | Pages | 207-212 |
| PubMed ID | 32446368 | Mgi Jnum | J:299924 |
| Mgi Id | MGI:6490829 | Doi | 10.1016/j.bbrc.2020.04.101 |
| Citation | Pauls SD, et al. (2020) SHIP interacts with adaptor protein Nck and restricts actin turnover in B cells. Biochem Biophys Res Commun 527(1):207-212 |
| abstractText | SH2 domain-containing inositol 5'-phosphatase (SHIP) has critical functions in regulating signal transduction. In additional to its lipid phosphatase activity, SHIP engages in multiple protein-protein interactions, which can serve to localize either SHIP or its binding partners to a particular subcellular domain. Knock-out and knock-down studies have elucidated that SHIP negatively regulates the accumulation of F-actin in leukocytes, usually resulting in inhibition of actin dependent cellular activities such as spreading and migration. Here, we demonstrate that overexpression of SHIP inhibits B cell antigen receptor (BCR)-mediated cell spreading in murine and human B cell lines. B cell stimulation via the BCR or pervanadate induces an interaction between SHIP and Nck, an adaptor protein known to promote actin polymerization. Using a fluorescence recovery after photobleaching (FRAP) assay, we demonstrate that overexpression of SHIP slows F-actin dynamics in BCR-stimulated B cells and this can be overcome by co-overexpression of Nck. Our data supports a role for SHIP in limiting actin turnover and suggests it may do so in part by sequestering Nck. |
