Signaling through receptors and scaffolds: independent interactions reduce combinatorial complexity.

ABSTRACT: After activation, many receptors and their adaptor proteins act as scaffolds displaying numerous docking sites and engaging multiple targets. The consequent assemblage of a variety of protein complexes results in a combinatorial increase in the number of feasible molecular species presenting different states of a receptor-scaffold signaling module. Tens of thousands of such microstates emerge even for the initial signal propagation events, greatly impeding a quantitative analysis of networks. Here, we demonstrate that the assumption of independence of molecular events occurring at distinct sites enables us to approximate a mechanistic picture of all possible microstates by a macrodescription of states of separate domains, i.e., macrostates that correspond to experimentally verifiable varia

SUBMITTER: Borisov NM 

PROVIDER: S-EPMC1366644 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature