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Chapter 50 - Assembly of Signaling Complexes for TNF Receptor Family Molecules
Book chapter

Chapter 50 - Assembly of Signaling Complexes for TNF Receptor Family Molecules

Gail A. Bishop and Bruce S. Hostager
Handbook of Cell Signaling, 2/e, pp.347-351
Elsevier Inc, Second Edition
2010
DOI: 10.1016/B978-0-12-374145-5.00050-4

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Abstract

This chapter summarizes and integrates currently available information on how the tumor necrosis factor receptor family (TNFR-F) of receptors assembles signaling complexes at the cell membrane, and how this may regulate cellular signaling pathways. A common property of TNFR-F molecules is their trimeric ligands, which can be found in both membrane-bound and soluble forms. The signaling complexes of several members of the TNFR family are assembled in specialized regions of the plasma membrane known as membrane microdomains or rafts. These regions of the plasma membrane, enriched in sphingolipids and cholesterol, are known to be sites of organization for various transmembrane signaling complexes. The activation-induced degradation of receptor-associated molecules is related to the downregulation of TNFR-F signaling. The activation of cells through CD30 or CD40 results in the degradation of TRAF2 and, in the case of CD40, TRAF3 as well. TRAFs may also act in the cytoplasm to influence the composition of TNFR-F signaling complexes at the cell membrane. Although CD40-bound TRAF6 is required to deliver certain CD40 signals, it has recently been shown that CD40 signaling also requires cytoplasmic TRAF6. It is thus possible that cytoplasmic TRAFs, by forming TRAF heterocomplexes that sequester other TRAFs from the cell membrane, regulate the formation of signaling complexes of TNFR-F molecules.

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