Biology:INF2
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Inverted formin-2 is a protein that in humans is encoded by the INF2 gene.[1][2] It belongs to the protein family called the formins. It has two splice isoforms, CAAX which localizes to the endoplasmic reticulum and non-CAAX which localizes to focal adhesions and the cytoplasm with enrichment at the Golgi.[3][4] INF2 plays a role in mitochondrial fission and dorsal stress fiber formation.[5] INF2 accelerates actin nucleation and elongation by interacting with barbed ends (fast-growing ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments.[6]
Clinical significance
It can be associated with Focal segmental glomerulosclerosis[7] and Charcot-Marie Tooth Disease.[8]
References
- ↑ "INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization". The Journal of Biological Chemistry 281 (36): 26754–67. September 2006. doi:10.1074/jbc.M604666200. PMID 16818491.
- ↑ "Entrez Gene: C14orf173 chromosome 14 open reading frame 173". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64423.
- ↑ "Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture". Molecular Biology of the Cell 22 (24): 4822–33. December 2011. doi:10.1091/mbc.E11-05-0457. PMID 21998196.
- ↑ "INF2 is an endoplasmic reticulum-associated formin protein". Journal of Cell Science 122 (Pt 9): 1430–40. May 2009. doi:10.1242/jcs.040691. PMID 19366733.
- ↑ "An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2". Science 339 (6118): 464–7. January 2013. doi:10.1126/science.1228360. PMID 23349293. Bibcode: 2013Sci...339..464K.
- ↑ "INF2-mediated severing through actin filament encirclement and disruption". Current Biology 24 (2): 156–64. January 2014. doi:10.1016/j.cub.2013.12.018. PMID 24412206.
- ↑ "Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis". Nature Genetics 42 (1): 72–6. January 2010. doi:10.1038/ng.505. PMID 20023659.
- ↑ "INF2 mutations in Charcot-Marie-Tooth disease with glomerulopathy". The New England Journal of Medicine 365 (25): 2377–88. December 2011. doi:10.1056/NEJMoa1109122. PMID 22187985. http://www.hal.inserm.fr/inserm-00919173/document.
Further reading
- "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research 16 (1): 55–65. January 2006. doi:10.1101/gr.4039406. PMID 16344560.
- "Formin' new ideas about actin filament generation". Proceedings of the National Academy of Sciences of the United States of America 101 (41): 14685–6. October 2004. doi:10.1073/pnas.0406317101. PMID 15466701. Bibcode: 2004PNAS..10114685B.
- "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics 84 (1): 205–10. July 2004. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology 21 (5): 566–9. May 2003. doi:10.1038/nbt810. PMID 12665801.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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