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Novel regulation of PLC? activity via its XY-linker.


ABSTRACT: The XY-linker region of somatic cell PLC (phospholipase)-?, -?, -? and -? isoforms confers potent catalytic inhibition, suggesting a common auto-regulatory role. Surprisingly, the sperm PLC? XY-linker does not mediate auto-inhibition. Unlike for somatic PLCs, the absence of the PLC? XY-linker significantly diminishes both in vitro PIP2 (phosphatidylinositol 4,5-bisphosphate) hydrolysis and in vivo Ca2+-oscillation-inducing activity, revealing evidence for a novel PLC? enzymatic mechanism.

SUBMITTER: Nomikos M 

PROVIDER: S-EPMC3195331 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature

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Novel regulation of PLCζ activity via its XY-linker.

Nomikos Michail M   Elgmati Khalil K   Theodoridou Maria M   Georgilis Athena A   Gonzalez-Garcia J Raul JR   Nounesis George G   Swann Karl K   Lai F Anthony FA  

The Biochemical journal 20110901 3


The XY-linker region of somatic cell PLC (phospholipase)-β, -γ, -δ and -ε isoforms confers potent catalytic inhibition, suggesting a common auto-regulatory role. Surprisingly, the sperm PLCζ XY-linker does not mediate auto-inhibition. Unlike for somatic PLCs, the absence of the PLCζ XY-linker significantly diminishes both in vitro PIP2 (phosphatidylinositol 4,5-bisphosphate) hydrolysis and in vivo Ca2+-oscillation-inducing activity, revealing evidence for a novel PLCζ enzymatic mechanism. ...[more]

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