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MBC in Press, published online ahead of print July 5, 2007
Mol. Biol. Cell 10.1091/mbc.E07-04-0306

A more recent version of this article appeared on September 1, 2007
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Submitted on April 5, 2007
Accepted on June 27, 2007

Serine phoshorylation of the Integrin {beta}4 Subunit Is Necessary for EGF Receptor-induced Hemidesmosome Disruption

Kevin Wilhelmsen, Sandy H.M. Litjens, Ingrid Kuikman, Coert Margadant, Jacco van Rheenen, and Arnoud Sonnenberg

Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands

Monitoring Editor: Mark Ginsberg

Hemidesmosomes (HDs) are multiprotein adhesion complexes that promote attachment of epithelial cells to the basement membrane. The binding of {alpha}6{beta}4 to plectin plays a central role in their assembly. We have defined three regions on {beta}4 that together harbor all the serine and threonine phosphorylation sites and show that three serines (S1356, S1360 and S1364), previously implicated in HD regulation, prevent the interaction of {beta}4 with the plectin actin-binding domain when phosphorylated. We have also established that EGF receptor activation, which is known to function upstream of HD disassembly, results in the phosphorylation of only one or more of these three residues and the partial disassembly of HDs in keratinocytes. Additionally, we show that S1360 and S1364 of {beta}4 are the only residues phosphorylated by PKC and PKA in cells, respectively. Taken together, our studies indicate that multiple kinases act in concert to breakdown the structural integrity of HDs in keratinocytes, which is primarily achieved through the phosphorylation of S1356, S1360 and S1364 on the {beta}4 subunit.

Address correspondence to: Arnoud Sonnenberg (a.sonnenberg{at}nki.nl)




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