| First Author | Keppler SJ | Year | 2018 |
| Journal | Cell Rep | Volume | 24 |
| Issue | 3 | Pages | 619-629 |
| PubMed ID | 30021160 | Mgi Jnum | J:270863 |
| Mgi Id | MGI:6278807 | Doi | 10.1016/j.celrep.2018.06.051 |
| Citation | Keppler SJ, et al. (2018) The Lack of WIP Binding to Actin Results in Impaired B Cell Migration and Altered Humoral Immune Responses. Cell Rep 24(3):619-629 |
| abstractText | Wiskott-Aldrich syndrome protein (WASp) is a main cytoskeletal regulator in B cells. WASp-interacting protein (WIP) binds to and stabilizes WASp but also interacts with actin. Using mice with a mutated actin binding domain of WIP (WIPDeltaABD), we here investigated the role of WIP binding to actin during B cell activation. We found an altered differentiation of WIPDeltaABD B cells and diminished antibody affinity maturation after immunization. Mechanistically, WIPDeltaABD B cells showed impaired B cell receptor (BCR)-induced PI3K signaling and actin reorganization, likely caused by diminished CD81 expression and altered CD19 dynamics on the B cell surface. WIPDeltaABD B cells displayed reduced in vivo motility, concomitantly with impaired chemotaxis and defective F-actin polarization, HS1 phosphorylation, and polarization of HS1 to F-actin-rich structures after CXCL12 stimulation in vitro. We thus concluded that WIP binding to actin, independent of its binding to WASp, is critical for actin cytoskeleton plasticity in B cells. |
