Residues neighboring an SH3-binding motif participate in the interaction in vivo.

ABSTRACT: In signaling networks, protein-protein interactions are often mediated by modular domains that bind short linear motifs. The motifs' sequences affect many factors, among them affinity and specificity, or the ability to bind strongly and to the appropriate partners. Using Deep Mutational Scanning to create a mutant library, and protein complementation assays to measure protein-protein interactions, we determined the in vivo binding strength of a library of mutants of a binding motif on the MAP kinase kinase Pbs2, which binds the SH3 domain of the osmosensor protein Sho1 in Saccharomyces cerevisiae. These measurements were made using the full-length endogenous proteins in their native cellular environment. We find that, along with residues within the canonical motif, many mutations in the re

SUBMITTER: Jordan DF 

PROVIDER: S-EPMC12505296 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature