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Cited by 1,373

The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.

Calcineurin: Form and Function

Rusnak, Frank, Mertz, Pamela·2000·Physiological Reviews

Abstract

Calcineurin is a eukaryotic Ca 2+- and calmodulin-dependent serine/threonine protein phosphatase. It is a heterodimeric protein consisting of a catalytic subunit calcineurin A, which contains an active site dinuclear metal center, and a tightly associated, myristoylated, Ca 2+-binding subunit, calcineurin B. The primary sequence of both subunits and heterodimeric quaternary structure is highly conserved from yeast to mammals. As a serine/threonine protein phosphatase, calcineurin participates in a number of cellular processes and Ca 2+-dependent signal transduction pathways. Calcineurin is potently inhibited by immunosuppressant drugs, cyclosporin A and FK506, in the presence of their respective cytoplasmic immunophilin proteins, cyclophilin and FK506-binding protein. Many studies have used these immunosuppressant drugs and/or modern genetic techniques to disrupt calcineurin in model organisms such as yeast, filamentous fungi, plants, vertebrates, and mammals to explore its biological function. Recent advances regarding calcineurin structure include the determination of its three-dimensional structure. In addition, biochemical and spectroscopic studies are beginning to unravel aspects of the mechanism of phosphate ester hydrolysis including the importance of the dinuclear metal ion cofactor and metal ion redox chemistry, studies which may lead to new calcineurin inhibitors. This review provides a comprehensive examination of the biological roles of calcineurin and reviews aspects related to its structure and catalytic mechanism.

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Crossref · 10.1152/physrev.2000.80.4.1483

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Metadata

Authors
Rusnak, F., & Mertz, P.
Venue
Physiological Reviews
Published
2000-01-10
Volume
80
Issue
4
Pages
1483-1521
ISSN
  • 0031-9333 (ISSN-L)
  • 1522-1210
OpenAlex
W2172196619
Cited by
1,373
References
13
FWCI
2.79
Type
journal article
Language
en
Open access
closed

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