Proteomics,Multiomics

Dataset Information

0

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.

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

altmetric image

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]

Similar Datasets

2020-05-18 | PXD019251 | Pride
2021-02-04 | PXD019751 | Pride
2020-06-18 | PXD015682 | Pride
2023-08-31 | PXD039289 | Pride
2023-09-15 | PXD025843 | Pride
2022-10-21 | PXD020636 | Pride
2022-12-08 | PXD030590 | Pride
2020-06-18 | PXD017996 | Pride
2021-12-15 | PXD025662 | Pride
2023-12-11 | PXD040144 | Pride