Title: | Complexes between STE5 and components of the pheromone-responsive mitogen-activated protein kinase module |
Author(s): | Marcus S; Polverino A; Barr M; Wigler M; |
Address: | "Cold Spring Harbor Laboratory, NY 11724" |
ISSN/ISBN: | 0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking) |
Abstract: | "We present genetic evidence for complex formation of STE5 and the STE11, STE7, and FUS3 protein kinases, the pheromone-responsive mitogen-activated protein kinase module of Saccharomyces cerevisiae. Interaction between STE5 and STE11 is not dependent on STE7, and interaction between STE5 and STE7 does not require STE11. The N-terminal regulatory domain of STE11 is both necessary and sufficient for interaction with STE5. Interaction between STE7 and STE11 is bridged by STE5, suggesting the formation of a multiprotein complex. We also demonstrate biochemical interaction between STE5 and STE11 by using a combination of bacterially expressed fusion proteins and extracts prepared from yeast. Our results suggest that STE5 is a scaffolding protein that facilitates interactions between components of the pheromone-responsive mitogen-activated protein kinase module. We further propose that such scaffolding proteins serve to inhibit cross-talk between functionally unrelated mitogen-activated protein kinase modules within the same cell" |
Keywords: | "*Adaptor Proteins, Signal Transducing Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism *Carrier Proteins Fungal Proteins/genetics/*metabolism MAP Kinase Kinase 1 MAP Kinase Kinase Kinases/metabolism Mitogen-Activated Protein Kinase Kinase;" |
Notes: | "MedlineMarcus, S Polverino, A Barr, M Wigler, M eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1994/08/02 Proc Natl Acad Sci U S A. 1994 Aug 2; 91(16):7762-6. doi: 10.1073/pnas.91.16.7762" |