PTRF

VALUE_ERROR (nil)
Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Polymerase I and transcript release factor, also known as Cavin1, Cavin-1 or PTRF, is a protein which in humans is encoded by the PTRF gene.

Function

PTRF (Cavin1) has been shown to be crucial for caveola formation and function.

Termination of RNA polymerase I catalyzed transcription is a 2-step process that involves pausing of transcription elongation and release of both the pre-ribosomal RNA and Pol I from the DNA template. The pausing is mediated by TTF1 and PTRF.

PTRF is a soluble protein containing putative leucine zipper, nuclear localization signal, and PEST domains.

Interactions

PTRF (Cavin1) forms trimers with Cavin2 and Cavin3 in caveola formation and has been shown to interact with other membrane associating proteins such as EHD2 and caveolins.

PTRF has been shown to interact with ZNF148.

Further reading

• Jansa P, Mason SW, Hoffmann-Rohrer U, Grummt I (May 1998). "Cloning and functional characterization of PTRF, a novel protein which induces dissociation of paused ternary transcription complexes". The EMBO Journal. 17 (10): 2855–64. doi:10.1093/emboj/17.10.2855. PMC 1170626. PMID 9582279.
• Hasegawa T, Takeuchi A, Miyaishi O, Xiao H, Mao J, Isobe K (April 2000). "PTRF (polymerase I and transcript-release factor) is tissue-specific and interacts with the BFCOL1 (binding factor of a type-I collagen promoter) zinc-finger transcription factor which binds to the two mouse type-I collagen gene promoters". The Biochemical Journal. 347 Pt 1 (Pt 1): 55–9. doi:10.1042/0264-6021:3470055. PMC 1220930. PMID 10727401.
• Aboulaich N, Vainonen JP, Strålfors P, Vener AV (October 2004). "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes". The Biochemical Journal. 383 (Pt 2): 237–48. doi:10.1042/BJ20040647. PMC 1134064. PMID 15242332.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM (September 2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Molecular & Cellular Proteomics. 4 (9): 1240–50. doi:10.1074/mcp.M500089-MCP200. PMID 15951569.
• Aboulaich N, Ortegren U, Vener AV, Strålfors P (November 2006). "Association and insulin regulated translocation of hormone-sensitive lipase with PTRF". Biochemical and Biophysical Research Communications. 350 (3): 657–61. doi:10.1016/j.bbrc.2006.09.094. PMID 17026959.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.