Ca2+-dependent protein acyltransferase DHHC21 controls activation of CD4+ T cells.

Abstract:

:Despite the recognized significance of reversible protein lipidation (S-acylation) for T cell receptor signal transduction, the enzymatic control of this post-translational modification in T cells remains poorly understood. Here, we demonstrate that DHHC21 (also known as ZDHHC21), a member of the DHHC family of mammalian protein acyltransferases, mediates T cell receptor-induced S-acylation of proximal T cell signaling proteins. Using Zdhhc21dep mice, which express a functionally deficient version of DHHC21, we show that DHHC21 is a Ca2+/calmodulin-dependent enzyme critical for activation of naïve CD4+ T cells in response to T cell receptor stimulation. We find that disruption of the Ca2+/calmodulin-binding domain of DHHC21 does not affect thymic T cell development but prevents differentiation of peripheral CD4+ T cells into Th1, Th2 and Th17 effector T helper lineages. Our findings identify DHHC21 as an essential component of the T cell receptor signaling machinery and define a new role for protein acyltransferases in regulation of T cell-mediated immunity.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Bieerkehazhi S,Fan Y,West SJ,Tewari R,Ko J,Mills T,Boehning D,Akimzhanov AM

doi

10.1242/jcs.258186

keywords:

["Calmodulin","Palmitoylation","Protein acyltransferase","S-acylation","T cell receptor"]

subject

Has Abstract

pub_date

2022-03-01 00:00:00

issue

5

eissn

0021-9533

issn

1477-9137

pii

268992

journal_volume

135

pub_type

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