A tripartite cooperative mechanism confers resistance of the protein kinase A catalytic subunit to dephosphorylation.

Authors

• Tung O Chan
• Roger S Armen
• Santosh Yadav
• Sushrut Shah
• Jin Zhang
• Brian C Tiegs
• Nikhil Keny
• Brian Blumhof
• Deepak A Deshpande
• Ulrich Rodeck
• Raymond B Penn

Publication/Presentation Date

3-6-2020

Abstract

Phosphorylation of specific residues in the activation loops of AGC kinase group (protein kinase A, G, and C families) is required for activity of most of these kinases, including the catalytic subunit of PKA (PKAc). Although many phosphorylated AGC kinases are sensitive to phosphatase-mediated dephosphorylation, the PKAc activation loop uniquely resists dephosphorylation, rendering it "constitutively" phosphorylated in cells. Previous biophysical experiments and structural modeling have suggested that the N-terminal myristoylation signal and the C-terminal F

Volume

295

Issue

10

First Page

3316

Last Page

3329

ISSN

1083-351X

Published In/Presented At

Chan, T. O., Armen, R. S., Yadav, S., Shah, S., Zhang, J., Tiegs, B. C., Keny, N., Blumhof, B., Deshpande, D. A., Rodeck, U., & Penn, R. B. (2020). A tripartite cooperative mechanism confers resistance of the protein kinase A catalytic subunit to dephosphorylation. The Journal of biological chemistry, 295(10), 3316–3329. https://doi.org/10.1074/jbc.RA119.010004

Disciplines

Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods

PubMedID

31964716

Department(s)

Administration and Leadership

Document Type

Article