Syndecan-4 core protein is sufficient for the assembly of focal adhesions and actin stress fibers. Academic Article uri icon

Overview

abstract

  • The formation of focal adhesions and actin stress fibers on fibronectin is dependent on signaling through (&bgr;)1 integrins and the heparan sulfate proteoglycan syndecan-4, and we have analyzed the requirement of the glycosaminoglycan chains of syndecan-4 during these events. Chinese hamster ovary cells with mutations in key enzymes of the glycanation process do not synthesize glycosaminoglycan chains and are unable to assemble actin stress fibers and focal contacts when cultured on fibronectin. Transfection of the mutant cells with a cDNA that encodes the core protein of chicken syndecan-4 leads to the production of unglycanated core protein. The overexpression of syndecan-4 core protein in these mutant cells increases cell spreading and is sufficient for these cells to assemble actin stress fibers and focal adhesions similar to wild-type cells seeded on fibronectin and vitronectin matrices. Syndecan-4 core protein colocalizes to focal contacts in mutant cells that have been transfected with the syndecan-4 core protein cDNA. These data indicate an essential role for the core protein of syndecan-4 in the generation of signals leading to actin stress fiber and focal contact assembly.

publication date

  • October 1, 1999

Research

keywords

  • Actins
  • Cell Adhesion
  • Membrane Glycoproteins
  • Proteoglycans

Identity

Scopus Document Identifier

  • 0032722310

Digital Object Identifier (DOI)

  • 10.1242/jcs.112.20.3433

PubMed ID

  • 10504292

Additional Document Info

volume

  • 112 ( Pt 20)