Proteomics

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A precisely positioned MED12 activation helix stimulates CDK8 kinase activity

ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study binary and ternary complexes involving cyclin-dependent kinase 8 (CDK8), cyclin-C, and subunit 12 of the Mediator complex (MED12). Cross-linking was performed using different cross-linking chemistries: (1) disuccinimidyl suberate (DSS); (2) a combination of pimelic acid dihydrazide (PDH) and the coupling reagent, DMTMM.

OTHER RELATED OMICS DATASETS IN: MODEL1109130000MODEL1311110000MODEL1909260003MODEL1311110001MODEL1909260004MODEL1703310000MODEL1909260005MODEL1909260006

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Leitner  

LAB HEAD: Claus-D. Kuhn

PROVIDER: PXD015394 | Pride | 2020-01-16

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
MED12_file_overview.xlsx Xlsx
MED12_results_DSS.xlsx Xlsx
MED12_results_PDH_DMTMM.xlsx Xlsx
aleitner_D1710_049.raw Raw
aleitner_D1710_050.raw Raw
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A precisely positioned MED12 activation helix stimulates CDK8 kinase activity.

Klatt Felix F   Leitner Alexander A   Kim Iana V IV   Ho-Xuan Hung H   Schneider Elisabeth V EV   Langhammer Franziska F   Weinmann Robin R   Müller Melanie R MR   Huber Robert R   Meister Gunter G   Kuhn Claus-D CD  

Proceedings of the National Academy of Sciences of the United States of America 20200127 6

The Mediator kinase module regulates eukaryotic transcription by phosphorylating transcription-related targets and by modulating the association of Mediator and RNA polymerase II. The activity of its catalytic core, cyclin-dependent kinase 8 (CDK8), is controlled by Cyclin C and regulatory subunit MED12, with its deregulation contributing to numerous malignancies. Here, we combine in vitro biochemistry, cross-linking coupled to mass spectrometry, and in vivo studies to describe the binding locat  ...[more]

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