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- W2227476670 abstract "Phosphorylase kinase (PhK) is a large hexadecameric complex that catalyzes the phosphorylation and activation of glycogen phosphorylase (GP). It consists in four copies each of a catalytic subunit ( γ )and three regulatory subunits ( α β δ ). δ corresponds to endogenous calmodulin, whereas little is known on the molecular architecture of the large α and β subunits, which probably arose from gene duplication. Here, using sensitive methods of sequence analysis we show that the C-terminal domain (named domain D) of these α and β subunits can be significantly related to calcineurin B-like (CBL) proteins. CBL are members of the EF-hand family that are involved in the regulation of plant-specific kinases of the CIPK/PKS family, and relieve autoinhibition of their target kinases by binding to their regulatory region. The relationship highlighted here suggests that PhK α and/or β domain D may be involved in a similar regulation mechanism a hypothesis which is supported by the experimental observation of a direct interaction between domain D of PhKα and the regulatory region of the γ subunit. This finding together the identification of significant similarities of domain D with the preceding domain C, may help to understand the molecular mechanism by which PhK α and/or β domain D might regulate PhK activity." @default.
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- W2227476670 date "2008-01-01" @default.
- W2227476670 modified "2023-10-13" @default.
- W2227476670 title "Calcineurin B-like domains in the large regulatory a/b subunits of phosphorylase kinase" @default.
- W2227476670 hasPublicationYear "2008" @default.
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