Five friends of methylated chromatin target of protein-arginine- methyltransferase[Prmt]-1 (Chtop), a complex linking arginine methylation to desumoylation

Pavlos Fanis, Nynke Gillemans, Ali Aghajanirefah, Farzin Pourfarzad, Jeroen Demmers, Fatemehsadat Esteghamat, Ratna K. Vadlamudi, Frank Grosveld, Sjaak Philipsen, Thamar B. Van Dijk

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

Chromatin target of Prmt1 (Chtop) is a vertebrate-specific chromatin-bound protein that plays an important role in transcriptional regulation. As its mechanism of action remains unclear, we identified Chtop-interacting proteins using a biotinylation-proteomics approach. Here we describe the identification and initial characterization of Five Friends of Methylated Chtop (5FMC). 5FMC is a nuclear complex that can only be recruited by Chtop when the latter is arginine-methylated by Prmt1. It consists of the co-activator Pelp1, the Sumo-specific protease Senp3, Wdr18, Tex10, and Las1L. Pelp1 functions as the core of 5FMC, as the other components become unstable in the absence of Pelp1. We show that recruitment of 5FMC to Zbp-89, a zinc-finger transcription factor, affects its sumoylation status and transactivation potential. Collectively, our data provide a mechanistic link between arginine methylation and (de)sumoylation in the control of transcriptional activity.

Original languageEnglish (US)
Pages (from-to)1263-1273
Number of pages11
JournalMolecular and Cellular Proteomics
Volume11
Issue number11
DOIs
StatePublished - Nov 2012

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Molecular Biology

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