ArticleScience advances2025
Conformational dynamics and multimodal interaction of Paxillin with the focal adhesion targeting domain.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Review
- Background-free quantitative phase imaging with adaptive-optics surface plasmon resonance holographic microscopy.Light, science & applications · 2026Article
- Prodigiosin Enhanced TMZ Chemosensitivity by Suppressing Focal Adhesion and Inhibiting Autophagy in Glioblastoma Cells.Biomolecules · 2026Article
- PEDV regulates trans-mammary epithelial migration of T cells in a CCR10/CCL28-dependent manner.Journal of virology · 2026Article
- Mapping the Ligand-dependent Remodeling of the Conformational Entropy Landscape in Neurotensin Receptor 1 by NMR-guided Molecular Simulations.bioRxiv : the preprint server for biology · 2026Article
- Differential PaxillinB dynamics at Dictyostelium cell-substrate adhesions.Biology open · 2025Article
- Targeting the hydrophobic pockets of FAK/PYK2 FAT domain: a highly effective inhibitory strategy suppressing tumor growth and eliminating metastasis.Cell communication and signaling : CCS · 2025Article
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8 authors.
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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 amino-terminal domain of PXN and the carboxyl-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-kilodalton multimodal complex with four major interconverting states. Although the complex is flexible, each state has unique sets of contacts involving disordered regions that are both highly represented in ensembles and conserved. PXN being a hub protein, the results provide a structural basis for understanding how shifts in the multistate equilibrium (e.g., through ligand binding and phosphorylation) may rewire cellular networks leading to phenotypic changes.
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