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Background: The protein kinase C (PKC) family of lipid-dependent serine/threonine kinases plays a central role in many intracellular eukaryotic signalling events. Members of the novel (δ, ε, η, θ) subclass of PKC isotypes lack the Ca 2+ dependence of the conventional PKC isotypes and have an N-terminal C2 domain, originally defined as V0 (variable domain zero). Biochemical data suggest...
Both the observed cis-inhibition and the proposed trans-activation of the insulin receptor tyrosine kinase help explain insulin signalling through its receptor.
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