Proteomics

Dataset Information

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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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Dataset's files

Source:
Action DRS
01_06_21_MPHDX3_PKD_M_3000s_3_0_01_16537.d.zip Other
01_06_21_MPHDX3_PKD_M_300s_3_0_01_16533.d.zip Other
01_06_21_MPHDX3_PKD_M_30s_3_0_01_16529.d.zip Other
01_06_21_MPHDX3_PKD_WT_3000s_3_0_01_16535.d.zip Other
01_06_21_MPHDX3_PKD_WT_300s_3_0_01_16531.d.zip Other
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Publications

PKD autoinhibition in <i>trans</i> regulates activation loop autophosphorylation in <i>cis</i>.

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 <i>trans</i>, whereby transient dimerization leads to the mutual phosph  ...[more]

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