Paxillin phase separation promotes focal adhesion assembly and integrin signaling.
J Cell Biol
; 223(4)2024 04 01.
Article
em En
| MEDLINE
| ID: mdl-38466167
ABSTRACT
Focal adhesions (FAs) are transmembrane protein assemblies mediating cell-matrix connection. Although protein liquid-liquid phase separation (LLPS) has been tied to the organization and dynamics of FAs, the underlying mechanisms remain unclear. Here, we experimentally tune the LLPS of PXN/Paxillin, an essential scaffold protein of FAs, by utilizing a light-inducible Cry2 system in different cell types. In addition to nucleating FA components, light-triggered PXN LLPS potently activates integrin signaling and subsequently accelerates cell spreading. In contrast to the homotypic interaction-driven LLPS of PXN in vitro, PXN condensates in cells are associated with the plasma membrane and modulated by actomyosin contraction and client proteins of FAs. Interestingly, non-specific weak intermolecular interactions synergize with specific molecular interactions to mediate the multicomponent condensation of PXN and are efficient in promoting FA assembly and integrin signaling. Thus, our data establish an active role of the PXN phase transition into a condensed membrane-associated compartment in promoting the assembly/maturation of FAs.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Adesões Focais
/
Paxilina
/
Separação de Fases
Limite:
Humans
Idioma:
En
Revista:
J Cell Biol
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
China