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Sci. STKE, 18 November 2003 REVIEWSOrganization and Functions of Interacting Domains for Signaling by Protein-Protein InteractionsElizabeth Buck and Ravi Iyengar* Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, 1 Gustave Levy Place, New York, NY 10029, USA. Gloss: This STKE review with two figures and 23 references discusses the molecular mechanisms by which information is transferred between interacting proteins in signaling pathways. Communication between protein partners in signaling pathways requires that the interactions between the partners be highly selective and that interactions be reversible. The reversibility of interactions ensures that interactions (and consequently communication) occur only when the system has received a signal at the receptor. The organization of interaction regions on signaling proteins into distinct domains that have specific and complementary spatial geometry in both proteins ensures that the interactions, even when of low affinity, can be highly selective. The ability of some of the interaction domains to actually transfer signals while others contribute only to overall binding affinity allows for information propagation through local conformational changes. Because this type of organization is observed in diverse proteins, such arrangements could constitute a general mechanism for information flow by noncovalent protein-protein interactions. *Corresponding author. Phone, 212-659-1707; fax, 212-831-0114; e-mail, ravi.iyengar{at}mssm.edu
Citation: E. Buck, R. Iyengar, Organization and Functions of Interacting Domains for Signaling by Protein-Protein Interactions. Sci. STKE 2003, re14 (2003). THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)
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