SHIP interacts with adaptor protein Nck and restricts actin turnover in B cells.
Autor: | Pauls SD; Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada. Electronic address: Samantha.Pauls@umanitoba.ca., Hou S; Department of Immunology, University of Manitoba, Winnipeg, Manitoba, Canada., Marshall AJ; Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada; Department of Immunology, University of Manitoba, Winnipeg, Manitoba, Canada. |
---|---|
Jazyk: | angličtina |
Zdroj: | Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2020 Jun 18; Vol. 527 (1), pp. 207-212. Date of Electronic Publication: 2020 May 01. |
DOI: | 10.1016/j.bbrc.2020.04.101 |
Abstrakt: | 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. Competing Interests: Declaration of competing interest The authors have no financial conflicts interest. (Copyright © 2020 Elsevier Inc. All rights reserved.) |
Databáze: | MEDLINE |
Externí odkaz: |