Activation of the essential kinase PDK1 by phosphoinositide-driven trans-autophosphorylation

Aleksandra Levina; Kaelin D. Fleming; John E. Burke; Thomas A. Leonard

doi:10.1038/s41467-022-29368-4

Nature Communications (Apr 2022)

Activation of the essential kinase PDK1 by phosphoinositide-driven trans-autophosphorylation

Aleksandra Levina,
Kaelin D. Fleming,
John E. Burke,
Thomas A. Leonard

Affiliations

Aleksandra Levina: Department of Structural and Computational Biology, Max Perutz Labs
Kaelin D. Fleming: Department of Biochemistry and Microbiology, University of Victoria
John E. Burke: Department of Biochemistry and Microbiology, University of Victoria
Thomas A. Leonard: Department of Structural and Computational Biology, Max Perutz Labs

DOI: https://doi.org/10.1038/s41467-022-29368-4
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 16

Abstract

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The essential protein kinase PDK1 is activated by phospoinositide-mediated dimerization and trans-autophosphorylation. Here, the authors show that in the absence of PIP3 or PI(3,4)P2 phosphoinositides, PDK1 is maintained in an inactive, autoinhibited conformation in the cytosol.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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