Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at leading edges polarizes neutrophils.

Abstract

A hallmark of neutrophil polarization is the back localization of active RHOA and phosphorylated myosin light chain (pMLC, also known as MYL2). However, the mechanism for the polarization is not entirely clear. Here, we show that FAM65B, a newly identified RHOA inhibitor, is important for the polarization. When FAM65B is phosphorylated, it binds to 14-3-3… (More)
DOI: 10.1242/jcs.161497

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