DIMERIZATION AS A REGULATORY MECHANISM IN SIGNAL TRANSDUCTION

Author:

Klemm Juli D.12,Schreiber Stuart L.12,Crabtree Gerald R.12

Affiliation:

1. Departments of Developmental Biology and Pathology, 1Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305;

2. Department of Chemical Biology, 2Howard Hughes Medical Institute, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138

Abstract

▪ Abstract  Dynamic protein-protein interactions are a key component of biological regulatory networks. Dimerization events—physical interactions between related proteins—represent an important subset of protein-protein interactions and are frequently employed in transducing signals from the cell surface to the nucleus. Importantly, dimerization between different members of a protein family can generate considerable functional diversity when different protein combinations have distinct regulatory properties. A survey of processes known to be controlled by dimerization illustrates the diverse physical and biological outcomes achieved through this regulatory mechanism. These include: facilitated proximity and orientation; differential regulation by heterodimerization; generation of temporal and spatial boundaries; enhancement of specificity; and regulated monomer-to-dimer transitions. Elucidation of these mechanisms has led to the design of new approaches to study and to manipulate signal transduction pathways.

Publisher

Annual Reviews

Subject

Immunology,Immunology and Allergy

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