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- Publisher
- Annual Reviews
- Copyright
- Copyright © 1998 by Annual Reviews. All rights reserved
- Subject
- Review Articles
- ISSN
- 0732-0582
- eISSN
- 1545-3278
- DOI
- 10.1146/annurev.immunol.16.1.569
- pmid
- 9597142
- Publisher site
- See Article on Publisher Site
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.
Journal
Annual Review of Immunology – Annual Reviews
Published: Apr 1, 1998