INF2

Inverted formin, FH2 and WH2 domain containing
Identifiers
Symbols	INF2 ; C14orf151; C14orf173; CMTDIE; FSGS5; pp9484
External IDs	OMIM: 610982 MGI: 1917685 HomoloGene: 82406 GeneCards: INF2 Gene
Gene ontology Molecular function • actin binding • Rho GTPase binding Cellular component • nucleus • cytoplasm • endoplasmic reticulum • perinuclear region of cytoplasm Biological process • actin cytoskeleton organization • regulation of cellular component size • regulation of mitochondrial fission Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	64423	70435
Ensembl	ENSG00000203485	ENSMUSG00000037679
UniProt	Q27J81	Q0GNC1
RefSeq (mRNA)	NM_001031714	NM_198411
RefSeq (protein)	NP_001026884	NP_940803
Location (UCSC)	Chr 14: 104.69 – 104.72 Mb	Chr 12: 112.59 – 112.62 Mb
PubMed search

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][5] INF2 plays a role in mitochondrial fission and dorsal stress fiber formation.^[5][6] INF2 accelerates actin nucleation and elongation by interacting with barbed ends (fast-growing ends) of actin filaments, but also accelerates depolymerization of actin through encircling and severing filaments.^[7]

Clinical significance

It can be associated with Focal segmental glomerulosclerosis^[8] and Charcot-Marie Tooth Disease.^[9]

References

1. Chhabra ES, Higgs HN (Sep 2006). "INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization". J Biol Chem 281 (36): 26754–67. doi:10.1074/jbc.M604666200. PMID 16818491.
2. "Entrez Gene: C14orf173 chromosome 14 open reading frame 173".
3. Ramabhadran, Vinay; Korobova, Farida; Rahme, Gilbert J.; Higgs, Henry N. (2011-12-01). "Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture". Molecular Biology of the Cell 22 (24): 4822–4833. doi:10.1091/mbc.E11-05-0457. ISSN 1939-4586. PMC 3237625. PMID 21998196.
4. Chhabra, Ekta Seth; Ramabhadran, Vinay; Gerber, Scott A.; Higgs, Henry N. (2009-05-01). "INF2 is an endoplasmic reticulum-associated formin protein". Journal of Cell Science 122 (Pt 9): 1430–1440. doi:10.1242/jcs.040691. ISSN 0021-9533. PMC 2721004. PMID 19366733.
5. Skau, Colleen T.; Plotnikov, Sergey V.; Doyle, Andrew D.; Waterman, Clare M. (2015-05-12). "Inverted formin 2 in focal adhesions promotes dorsal stress fiber and fibrillar adhesion formation to drive extracellular matrix assembly". Proceedings of the National Academy of Sciences of the United States of America 112 (19): E2447–2456. doi:10.1073/pnas.1505035112. ISSN 1091-6490. PMC 4434736. PMID 25918420.
6. Korobova, Farida; Ramabhadran, Vinay; Higgs, Henry N. (2013-01-25). "An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2". Science (New York, N.Y.) 339 (6118): 464–467. doi:10.1126/science.1228360. ISSN 1095-9203. PMC 3843506. PMID 23349293.
7. Gurel, Pinar S.; Ge, Peng; Grintsevich, Elena E.; Shu, Rui; Blanchoin, Laurent; Zhou, Z. Hong; Reisler, Emil; Higgs, Henry N. (2014-01-20). "INF2-mediated severing through actin filament encirclement and disruption". Current biology: CB 24 (2): 156–164. doi:10.1016/j.cub.2013.12.018. ISSN 1879-0445. PMC 3992431. PMID 24412206.
8. Brown EJ, Schlöndorff JS, Becker DJ, Tsukaguchi H, Uscinski AL, Higgs HN, Henderson JM, Pollak MR. (Jan 2010). "Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis". Nature Genetics 42 (1): 72–6. doi:10.1038/ng.505. PMC 2980844. PMID 20023659.
9. Boyer, Olivia; Nevo, Fabien; Plaisier, Emmanuelle; Funalot, Benoit; Gribouval, Olivier; Benoit, Geneviève; Huynh Cong, Evelyne; Arrondel, Christelle; Tête, Marie-Josèphe (2011-12-22). "INF2 mutations in Charcot-Marie-Tooth disease with glomerulopathy". The New England Journal of Medicine 365 (25): 2377–2388. doi:10.1056/NEJMoa1109122. ISSN 1533-4406. PMID 22187985.

Further reading

• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Bindschadler M, McGrath JL (2004). "Formin' new ideas about actin filament generation". Proc. Natl. Acad. Sci. U.S.A. 101 (41): 14685–6. doi:10.1073/pnas.0406317101. PMC 522045. PMID 15466701.
• Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome". Science 291 (5507): 1304–51. doi:10.1126/science.1058040. PMID 11181995.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.