The structural requirements for ceramide activation of serine-threonine protein phosphatases
نویسندگان
چکیده
منابع مشابه
The structural requirements for ceramide activation of serine-threonine protein phosphatases.
The protein phosphatases1 (PP1) and 2A (PP2A) serve as ceramide-activated protein phosphatases (CAPP). In this study, the structural requirements for interaction between ceramide and CAPP were determined. D-erythro-C(6) ceramide activated the catalytic subunit of PP2A (PP2Ac) approximately 3-fold in a stereospecific manner. In contrast, saturation of the 4-5 double bond, producing D-erythro-dih...
متن کاملSerine/threonine protein phosphatases.
1 (1-1) and inhibitor-2 (1-2), and preferentially dephosphorylate the /3-subunit of phosphorylase kinase, whereas type-2 phosphatases are insensitive to the heat-stable inhibitors and preferentially dephosphorylate the x-subunit of phosphorylase kinase [1,2]. Type-2 phosphatases can be further subdivided into spontaneously active (PP2A), Ca2l-dependent (PP2B) and Mg2+dependent (PP2C) classes. T...
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Modulation of exocytosis is integral to the regulation of cellular signalling, and a variety of disorders (such as epilepsy, hypertension, diabetes and asthma) are closely associated with pathological modulation of exocytosis. Emerging evidence points to protein phosphatases as key regulators of exocytosis in many cells and, therefore, as potential targets for the design of novel therapies to t...
متن کاملThe Structure and Topology of Protein Serine/Threonine Phosphatases
Structural studies of the two families of protein phosphatases responsible for dephosphorylating serine and threonine residues have revealed that, although these families are unrelated in sequence, the architecture of their catalytic domains is remarkably similar and distinct from the protein tyrosine phosphatases. The diversity of structure within the PPP and PPM families is generated by regul...
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With the recent clinical success of drugs targeting protein kinase activity, drug discovery efforts are focusing on the role of reversible protein phosphorylation in disease states. The activity of protein phosphatases, enzymes that oppose protein kinases, can also be manipulated to alter cellular signaling for therapeutic benefits. In this review, we present protein serine/threonine phosphatas...
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ژورنال
عنوان ژورنال: Journal of Lipid Research
سال: 2004
ISSN: 0022-2275
DOI: 10.1194/jlr.m300347-jlr200