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Phosphoprotein Inhibitor CPI-17 Specificity Depends on Allosteric Regulation of Protein Phosphatase-...

Phosphoprotein Inhibitor CPI-17 Specificity Depends on Allosteric Regulation of Protein Phosphatase-...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_3372359

Phosphoprotein Inhibitor CPI-17 Specificity Depends on Allosteric Regulation of Protein Phosphatase-1 by Regulatory Subunits

About this item

Full title

Phosphoprotein Inhibitor CPI-17 Specificity Depends on Allosteric Regulation of Protein Phosphatase-1 by Regulatory Subunits

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2004-06, Vol.101 (24), p.8888-8893

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Inhibition of myosin phosphatase is critical for agonist-induced contractility of vascular smooth muscle. The protein CPI-17 is a phosphorylation-dependent inhibitor of myosin phosphatase and, in response to agonists, Thr-38 is phosphorylated by protein kinase C, producing a > 1,000-fold increase in inhibitory potency. Here, we addressed how CPI-17...

Alternative Titles

Full title

Phosphoprotein Inhibitor CPI-17 Specificity Depends on Allosteric Regulation of Protein Phosphatase-1 by Regulatory Subunits

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_jstor_primary_3372359

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_3372359

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0307812101

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