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PKD autoinhibition in trans prevents activation loop autophosphorylation in cis

ABSTRACT: HDX-MS analysis of the kinase domain of PKD1, showing that it forms an inactive dimer

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD033139 | Pride | 2023-02-22

REPOSITORIES: Pride

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PKD autoinhibition in trans regulates activation loop autophosphorylation in cis.

Reinhardt Ronja R Hirzel Kai K Link Gisela G Eisler Stephan A SA Hägele Tanja T Parson Matthew A H MAH Burke John E JE Hausser Angelika A Leonard Thomas A TA

Proceedings of the National Academy of Sciences of the United States of America 20230206 7

Phosphorylation is a ubiquitous mechanism by which signals are transduced in cells. Protein kinases, enzymes that catalyze the phosphotransfer reaction are, themselves, often regulated by phosphorylation. Paradoxically, however, a substantial fraction of more than 500 human protein kinases are capable of catalyzing their own activation loop phosphorylation. Commonly, these kinases perform this autophosphorylation reaction in trans, whereby transient dimerization leads to the mutual phosph ...[more]

PMID: 36745811

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