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Protein interaction domains and biological complexity
Author(s) -
Pawson Tony
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a455-c
Subject(s) - function (biology) , mechanism (biology) , protein–protein interaction , signal transducing adaptor protein , computational biology , biology , computer science , microbiology and biotechnology , signal transduction , physics , quantum mechanics
Many aspects of cellular function are controlled through regulated protein‐protein interactions, mediated by dedicated interaction domains. Indeed cell surface receptors are frequently coupled to intracellular targets through adaptor proteins, composed exclusively of interaction domains. Genetic, biochemical and proteomic data will be presented in support of the argument that such adaptors can have very versatile functions. Although superficially simple, adaptors can nonetheless control complex biological systems. Furthermore, the acquisition of new interaction sequences by pre‐existing adaptors may represent a common mechanism for the evolution of new biological functions.