4f2h
Structure of the minimal Ste5 VWA domain subject to autoinhibition by the Ste5 PH domainStructure of the minimal Ste5 VWA domain subject to autoinhibition by the Ste5 PH domain
Structural highlights
Function[STE5_YEAST] Component of the pheromone signal transduction pathway. It mediates pheromone signals acting between STE20 and STE11. It is absolutely required for pheromone-induced transcription of FUS1. May play a role in cell-cycle arrest in response to pheromone. Publication Abstract from PubMedCells reuse signaling proteins in multiple pathways, raising the potential for improper crosstalk. Scaffold proteins are thought to insulate against such miscommunication by sequestering proteins into distinct physical complexes. We show that the scaffold protein Ste5, which organizes the yeast mating mitogen-activated protein (MAP) kinase pathway, does not use sequestration to prevent misactivation of the mating response. Instead, Ste5 appears to use a conformation mechanism: Under basal conditions, intramolecular interaction of the PH domain with the VWA domain blocks the ability to coactivate the mating-specific MAPK, Fus3. Pheromone-induced membrane binding of Ste5 triggers release of this autoinhibition. Thus, in addition to serving as a conduit guiding kinase communication, Ste5 directly receives input information to decide if and when signal can be transmitted to mating output. Conformational Control of the Ste5 Scaffold Protein Insulates Against MAP Kinase Misactivation.,Zalatan JG, Coyle SM, Rajan S, Sidhu SS, Lim WA Science. 2012 Aug 9. PMID:22878499[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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