Dissecting phospho-motif-dependent Shc1 interactome using long synthetic protein fragments.

ABSTRACT: Activated receptor tyrosine kinases (RTKs) rely on the assembly of signaling proteins into high-dimensional protein complexes for signal transduction. Shc1, a prototypical scaffold protein, plays a pivotal role in directing phosphotyrosine (pY)-dependent protein complex formation for numerous RTKs typically through its two pY-binding domains. The three conserved pY sites within its CH1 region (Shc1^CH1) hold particular significance due to their substantial contribution to its functions. However, how Shc1 differentially utilizes these sites to precisely coordinate protein complex assembly remains unclear. Here, we employed multiple peptide ligation techniques to synthesize an array of long protein fragments (107 amino acids) covering a significant portion of the Shc1^CH1

SUBMITTER: Chen P 

PROVIDER: S-EPMC11342145 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature