Proteomics

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Interactions of CDK19 with MED12 and cyclin-C assessed by chemical cross-linking mass spectrometry

ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study binary and ternary complexes involving cyclin-dependent kinase 19 (CDK19), cyclin-C, and an N-terminal fragment of subunit 12 of the Mediator complex (MED12 1-100). Cross-linking was performed using disuccinimidyl suberate (DSS). These results were generated in the context of the study published as Klatt et al., A precisely positioned MED12 activation helix stimulates CDK8 kinase activity, Proc. Natl. Acad. Sci. USA 2020 (DOI: 10.1073/pnas.1917635117) with the associated data set PXD015394, but were not included in the article.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Leitner  

LAB HEAD: Claus-D. Kuhn

PROVIDER: PXD019251 | Pride | 2020-05-18

REPOSITORIES: Pride

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Cdk19_2mer_sh.fasta Fasta
Cdk19_3mer_sh.fasta Fasta
Cdk19_file_overview.xlsx Xlsx
Cdk19_results.xlsx Xlsx
aleitner_D1901_203.raw Raw
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Publications

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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