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The Drosophila CoREST interactome

ABSTRACT: Affinity purification of dCoREST-interacting proteins from Drosophila melanogaster S2 cell nuclear extracts. An antibody recognizing both dCoREST isoforms was used to affinity purify proteins interacting with endogenous dCoREST from S2 nuclear extract. In addition, nuclear extracts from S2 cell lines ectopically expressing the FLAG-tagged dCoREST-L isoform and the FLAG-tagged dCoREST-M isoform, respectively, were subjected to anti-FLAG affinity purification to purify isoform specific dCoREST-interacting proteins.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

SUBMITTER: Ignasi Forne

LAB HEAD: Prof. Dr. Alexander Brehm

PROVIDER: PXD014857 | Pride | 2019-11-11

REPOSITORIES: Pride

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Publications

Distinct CoREST complexes act in a cell-type-specific manner.

Mačinković Igor I Theofel Ina I Hundertmark Tim T Kovač Kristina K Awe Stephan S Lenz Jonathan J Forné Ignasi I Lamp Boris B Nist Andrea A Imhof Axel A Stiewe Thorsten T Renkawitz-Pohl Renate R Rathke Christina C Brehm Alexander A

Nucleic acids research 20191201 22

CoREST has been identified as a subunit of several protein complexes that generate transcriptionally repressive chromatin structures during development. However, a comprehensive analysis of the CoREST interactome has not been carried out. We use proteomic approaches to define the interactomes of two dCoREST isoforms, dCoREST-L and dCoREST-M, in Drosophila. We identify three distinct histone deacetylase complexes built around a common dCoREST/dRPD3 core: A dLSD1/dCoREST complex, the LINT complex ...[more]

PMID: 31701127

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