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The Lack of WIP Binding to Actin Results in Impaired B Cell Migration and Altered Humoral Immune Responses.

Abstract：

: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 (WIPΔABD), we here investigated the role of WIP binding to actin during B cell activation. We found an altered differentiation of WIPΔABD B cells and diminished antibody affinity maturation after immunization. Mechanistically, WIPΔABD 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. WIPΔABD 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.

journal_name

Cell Rep

journal_title

Cell reports

authors

Keppler SJ,Burbage M,Gasparrini F,Hartjes L,Aggarwal S,Massaad MJ,Geha RS,Bruckbauer A,Batista FD

doi

10.1016/j.celrep.2018.06.051

subject

Has Abstract

pub_date

2018-07-17 00:00:00

pages

619-629

issue

3

issn

2211-1247

pii

S2211-1247(18)30961-6

journal_volume

24

pub_type

杂志文章

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