Subject collection: Adhesion
- Distinct focal adhesion protein modules control different aspects of mechanotransduction
Summary: Quantitative fluorescence microscopy shows that focal adhesions are composed of functional protein modules, which control distinct aspects of mechanotransduction.
- Localization of phosphorylated connexin 43 using serial section immunogold electron microscopy
Highlighted Article: Here, we show how new 3D electron microscopy techniques can be extended to investigate ultrastructural protein localization in order to advance insight into mechanisms of gap junction internalization.
- Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes
Summary: Development is more sensitive to gain of vinculin activity than its loss, and vinculin can promote cytoplasmic adhesion complexes independently of the usual integrin cue.
- Cell coupling mediated by connexin 26 selectively contributes to reduced adhesivity and increased migration
Summary: Gap junction expression has been linked to enhanced metastasis and cell migration. We show here that Cx26 gap junctions selectively enhance cell migration by disrupting N-cadherin-based cell adhesion in HeLa cells.
- Prickle1 promotes focal adhesion disassembly in cooperation with the CLASP–LL5β complex in migrating cells
Highlighted Article: Prickle localizes adjacent to focal adhesions and regulates microtubule targeting to focal adhesions in cooperation with CLASPs and LL5β, thereby promoting focal adhesion disassembly to stimulate cell migration.
- Molecular organization of the desmosome as revealed by direct stochastic optical reconstruction microscopy
Highlighted Article: The nanoscale organization of proteins in the desmosome, a structure mediating strong cell–cell adhesion, is elucidated by dSTORM super-resolution fluorescence microscopy.
- LAR protein tyrosine phosphatase regulates focal adhesions through CDK1
Highlighted Article: We demonstrate that LAR, a receptor tyrosine phosphatase, signals through CDK1 to promote adhesion complex formation and adhesion to the extracellular matrix.
- The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits
Summary: The extracellular O-glycosylated domain of FXYD5 impairs adhesion by interfering with intercellular interactions between Na,K-ATPase β1 subunits. Four conserved β1 residues, including Y199, are crucial in this process.
- Cortactin is a scaffolding platform for the E-cadherin adhesion complex and is regulated by protein kinase D1 phosphorylation
Summary: Cortactin and its phosphorylation by protein kinase D1 at S298 modulate E-cadherin adhesion complex composition and F-actin linkage during ligation and dissolution of adherence junctions.
- Heparin interacts with the adhesion GPCR GPR56, reduces receptor shedding, and promotes cell adhesion and motility
Summary: GPR56 is an adhesion GPCR that we show interacts with heparin through heparin-interacting motifs. This interaction regulates cell adhesion, which has possible implications for diseases such as cancer.