title: Dimerization as a regulatory mechanism in signal transduction.
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.
authors.affiliation: Howard Hughes Medical Institute, Department of Developmental Biology, Stanford University Medical School, California 94305, USA.
authors.forename: J D
authors.initials: JD
authors.lastname: Klemm
authors.forename: S L
authors.initials: SL
authors.lastname: Schreiber
authors.forename: G R
authors.initials: GR
authors.lastname: Crabtree
mesh_terms: D000818:Animals; D019281:Dimerization; D006801:Humans; D011485:Protein Binding; D015398:Signal Transduction / Q000502:physiology*