Phosphorylation of threonine 1736 in the C-terminal tail of integrin β4 contributes to hemidesmosome disassembly

@inproceedings{Frijns2012PhosphorylationOT,
  title={Phosphorylation of threonine 1736 in the C-terminal tail of integrin β4 contributes to hemidesmosome disassembly},
  author={Evelyne Frijns and Ingrid Kuikman and Sandy H. M. Litjens and Marcel Raspe and Kees Jalink and Michael O Ports and Kevin Wilhelmsen and Arnoud Sonnenberg},
  booktitle={Molecular biology of the cell},
  year={2012}
}
During wound healing, hemidesmome disassembly enables keratinocyte migration and proliferation. Hemidesmosome dynamics are altered downstream of epidermal growth factor (EGF) receptor activation, following the phosphorylation of integrin β4 residues S1356 and S1364, which reduces the interaction with plectin; however, this event is insufficient to drive complete hemidesmome disassembly. In the studies reported here, we used a fluorescence resonance energy transfer-based assay to demonstrate… CONTINUE READING
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Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the beta4 subunit and plectin at multiple molecular sites

  • GA Rezniczek, JM de Pereda, S Reipert, G Wiche
  • J Cell Biol
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