title: Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation.
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.
authors.affiliation: Department of Cell Biology, Erasmus MC, 3000 CA, Rotterdam, The Netherlands.
authors.forename: Pavlos
authors.initials: P
authors.lastname: Fanis
authors.forename: Nynke
authors.initials: N
authors.lastname: Gillemans
authors.forename: Ali
authors.initials: A
authors.lastname: Aghajanirefah
authors.forename: Farzin
authors.initials: F
authors.lastname: Pourfarzad
authors.forename: Jeroen
authors.initials: J
authors.lastname: Demmers
authors.forename: Fatemehsadat
authors.initials: F
authors.lastname: Esteghamat
authors.forename: Ratna K
authors.initials: RK
authors.lastname: Vadlamudi
authors.forename: Frank
authors.initials: F
authors.lastname: Grosveld
authors.forename: Sjaak
authors.initials: S
authors.lastname: Philipsen
authors.forename: Thamar B
authors.initials: TB
authors.lastname: van Dijk
mesh_terms: D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism*; D056970:Co-Repressor Proteins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D005786:Gene Expression Regulation; D006801:Humans; D008745:Methylation; D051379:Mice; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D011485:Protein Binding; D055550:Protein Stability; D011484:Protein-Arginine N-Methyltransferases / Q000378:metabolism*; D058207:Sumoylation; D014157:Transcription Factors / Q000378:metabolism*
chemical_list: C541075:CHTOP protein, human; D002843:Chromatin; D056970:Co-Repressor Proteins; C554294:FOP protein, mouse; C552426:Las1L protein, human; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; C438485:PELP1 protein, human; C558247:TEX10 protein, human; D014157:Transcription Factors; C558249:WDR18 protein, human; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases; D010447:Peptide Hydrolases; D003546:Cysteine Endopeptidases; C499718:SENP3 protein, human; C492190:Senp3 protein, mouse