| CAVIN1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | CAVIN1, CAVIN, CGL4, cavin-1, FKSG13, PTRF, polymerase I and transcript release factor, caveolae associated protein 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603198 MGI: 1277968 HomoloGene: 7499 GeneCards: CAVIN1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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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.[5][6]
Function
PTRF (Cavin1) has been shown to be crucial for caveola formation and function.[7] Deformation caveolae promotes the translocation of cavin-1 from caveolae to the nucleus[8]
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.[9][10]
PTRF is a soluble protein containing putative leucine zipper, nuclear localization signal, and PEST domains.[11]
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.[12]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000177469 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000004044 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Entrez Gene: PTRF polymerase I and transcript release factor".
- ↑ "CAVIN1 Symbol Report | HUGO Gene Nomenclature Committee". www.genenames.org. Retrieved 2017-05-30.
- ↑ Hill MM, Bastiani M, Luetterforst R, Kirkham M, Kirkham A, Nixon SJ, et al. (January 2008). "PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and function". Cell. 132 (1): 113–124. doi:10.1016/j.cell.2007.11.042. PMC 2265257. PMID 18191225.
- ↑ Qifti A, Balaji S, Scarlata S (June 2022). "Deformation of caveolae impacts global transcription and translation processes through relocalization of cavin-1". The Journal of Biological Chemistry. 298 (6): 102005. doi:10.1016/j.jbc.2022.102005. PMC 9168624. PMID 35513070.
- ↑ Mason SW, Sander EE, Grummt I (January 1997). "Identification of a transcript release activity acting on ternary transcription complexes containing murine RNA polymerase I". The EMBO Journal. 16 (1): 163–172. doi:10.1093/emboj/16.1.163. PMC 1169623. PMID 9009277.
- ↑ 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): 2855–2864. doi:10.1093/emboj/17.10.2855. PMC 1170626. PMID 9582279.
- ↑ 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): 237–248. doi:10.1042/BJ20040647. PMC 1134064. PMID 15242332.
- ↑ Kovtun O, Tillu VA, Ariotti N, Parton RG, Collins BM (April 2015). "Cavin family proteins and the assembly of caveolae". Journal of Cell Science. 128 (7): 1269–1278. doi:10.1242/jcs.167866. PMC 4379724. PMID 25829513.
- ↑ 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): 55–59. doi:10.1042/0264-6021:3470055. PMC 1220930. PMID 10727401.
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): 2855–2864. 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): 55–59. 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): 237–248. doi:10.1042/BJ20040647. PMC 1134064. PMID 15242332.
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, et al. (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
- 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): 1240–1250. 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): 657–661. 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): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
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