Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition.

ABSTRACT: Intrinsically disordered cytoplasmic domains of T cell receptor (TCR) signaling subunits including zeta(cyt) and CD3epsilon(cyt) all contain one or more copies of an immunoreceptor tyrosine-based activation motif (ITAM), tyrosine residues of which are phosphorylated upon receptor triggering. Membrane binding-induced helical folding of zeta(cyt) and CD3epsilon(cyt) ITAMs is thought to control TCR activation. However, the question whether or not lipid binding of zeta(cyt) and CD3epsilon(cyt) is necessarily accompanied by a folding transition of ITAMs remains open. In this study, we investigate whether the membrane binding mechanisms of zeta(cyt) and CD3epsilon(cyt) depend on the membrane model used. Circular dichroic and fluorescence data indicate that binding of zeta(cyt) and CD3epsilon(cyt

SUBMITTER: Sigalov AB 

PROVIDER: S-EPMC2795782 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature