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Immunol Rev. 2009 Nov;232(1):218-28. doi: 10.1111/j.1600-065X.2009.00827.x.

SLAP, a regulator of immunoreceptor ubiquitination, signaling, and trafficking.

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1
National Jewish Health, Denver, CO 80206, USA. dragonel@njhealth.org

Abstract

Src-like adapter proteins (SLAP and SLAP-2) constitute a family of proteins that are expressed in a variety of cell types but are studied most extensively in lymphocytes. They have been shown to associate with proximal components of the T-cell receptor (TCR) and B-cell receptor (BCR) signaling complexes. An interaction of SLAP with c-Cbl leads to the ubiquitination and degradation of phosphorylated components of the TCR- and BCR-signaling complexes. The absence of this process in immature SLAP-deficient T and B cells leads to increased immunoreceptor levels due to decreased intracellular retention and degradation. We propose a model in which SLAP-dependent regulation of immunoreceptor levels allows for finer control of immunoreceptor signaling. Thus, SLAP functions to dampen immunoreceptor signaling, thereby influencing lymphocyte development and repertoire selection.

[Indexed for MEDLINE]

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