Conformational dynamics and multi-modal interaction of Paxillin with the Focal Adhesion Targeting Domain.

ABSTRACT: Paxillin (PXN) and focal adhesion kinase (FAK) are two major components of the focal adhesion complex, a multiprotein structure linking the intracellular cytoskeleton to the cell exterior. The interaction between the disordered N-terminal domain of PXN and the C-terminal targeting domain of FAK (FAT) is necessary and sufficient for localizing FAK to focal adhesions. Furthermore, PXN serves as a platform for recruiting other proteins that together control the dynamic changes needed for cell migration and survival. Here, we show that the PXN N-domain undergoes significant compaction upon FAT binding, forming a 48-kDa multi-modal complex with four major interconverting states. Although the complex is flexible, each state has unique sets of contacts involving disordered regions that are both h

SUBMITTER: Bhattacharya S 

PROVIDER: S-EPMC11722443 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature