Regulation of hemidesmosome disassembly by growth factor receptors

C Margadant, E Frijns, K Wilhelmsen… - Current opinion in cell …, 2008 - Elsevier
C Margadant, E Frijns, K Wilhelmsen, A Sonnenberg
Current opinion in cell biology, 2008Elsevier
Hemidesmosomes (HDs) promote the stable adhesion of basal epithelial cells to the
underlying basement membrane (BM). Critical for the mechanical stability of the HD is the
interaction between integrin α6β4 and plectin, which is destabilized when HD disassembly
is required, for instance, to allow keratinocyte migration during wound healing. Growth
factors such as epidermal growth factor (EGF) can trigger HD disassembly and induce
phosphorylation of the β4 intracellular domain. Whereas tyrosine phosphorylation appears …
Hemidesmosomes (HDs) promote the stable adhesion of basal epithelial cells to the underlying basement membrane (BM). Critical for the mechanical stability of the HD is the interaction between integrin α6β4 and plectin, which is destabilized when HD disassembly is required, for instance, to allow keratinocyte migration during wound healing. Growth factors such as epidermal growth factor (EGF) can trigger HD disassembly and induce phosphorylation of the β4 intracellular domain. Whereas tyrosine phosphorylation appears to mediate cooperation with growth factor signaling pathways and invasion in carcinoma cells, serine phosphorylation seems the predominant mechanism for regulating HD destabilization. Here, we discuss recent advances that shed light on the residues involved, the identity of the kinases that phosphorylate them, and the interactions that become disrupted by these phosphorylations.
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