Abstract
Protein kinase C (PKC) has been implicated in integrin-mediated spreading and migration. In mammary epithelial cells there is a partial co-localization between beta1 integrin and PKCalpha. This reflects complexes between these proteins as demonstrated by fluorescense resonance energy transfer (FRET) monitored by fluorescence lifetime imaging microscopy and also by coprecipitation. Constitutive complexes are observed for the intact PKCalpha and also form with the regulatory domain in an activation-dependent manner. Expression of PKCalpha causes upregulation of beta1 integrin on the cell surface, whereas stimulation of PKC induces internalization of beta1 integrin. The integrin initially traffics to an endosomal compartment in a Ca(2+)/PI 3-kinase/dynamin I-dependent manner and subsequently enters an endocytic recycling pathway. This induction of endocytosis by PKCalpha is a function of activity and is not observed for the regulatory domain. PKCalpha, but not PKCalpha regulatory domain expression stimulates migration on beta1 integrin substrates. This PKCalpha-enhanced migratory response is inhibited by blockade of endocytosis.
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