| Autor: |
Ivaska, Johanna, Whelan, Richard D. H., Watson, Rose, Parker, Peter J. |
| Předmět: |
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| Zdroj: |
EMBO Journal; 7/15/2002, Vol. 21 Issue 14, p3608-3619, 12p |
| Abstrakt: |
Protein kinase C (PKC) has been implicated in β1 integrin-mediated cell migration. Expression of the novel PKC isoform, PKC∊, in PKC∊-/- cells is shown here to stimulate directional migration of cells towards β1 integrin substrates in a manner dependent on PKC catalytic activity. On PKC inhibition, integrin β1 and PKC∊ become reversibly trapped in a tetraspanin (CD81)-positive intracellular compartment, correlating with reduced haptotaxis. Immunofluorescence and pulse labelling studies indicate that this is a previously uncharacterized recycling compartment trapped by inhibition of PKC. Electron microscopy demonstrated the co-localization of PKC∊ and integrin β1 on the vesicular membranes. Finally, using a reconstituted in vitro system, the dissociation of PKC∊ from these vesicles is shown to be dependent on both the presence of cytosolic components and energy, and on PKC catalytic activity. The evidence presented indicates that PKC∊ controls an internal traffic step that under uninhibited conditions permits the recycling of β1 integrin, contributing to cell motility. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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