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Aliases INF2, C14orf151, C14orf173, CMTDIE, FSGS5, pp9484, inverted formin, FH2 and WH2 domain containing
External IDs MGI: 1917685 HomoloGene: 82406 GeneCards: INF2
RNA expression pattern
PBB GE C14orf173 218144 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 14: 104.69 – 104.72 Mb Chr 12: 112.59 – 112.62 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Inverted formin-2 is a protein that in humans is encoded by the INF2 gene.[3][4] 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.[5][6][7] INF2 plays a role in mitochondrial fission and dorsal stress fiber formation.[7][8] 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.[9]

Clinical significance[edit]

It can be associated with Focal segmental glomerulosclerosis[10] and Charcot-Marie Tooth Disease.[11]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Chhabra ES, Higgs HN (September 2006). "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. doi:10.1074/jbc.M604666200. PMID 16818491. 
  4. ^ "Entrez Gene: C14orf173 chromosome 14 open reading frame 173". 
  5. ^ Ramabhadran V, Korobova F, Rahme GJ, Higgs HN (December 2011). "Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture". Molecular Biology of the Cell. 22 (24): 4822–33. doi:10.1091/mbc.E11-05-0457. PMC 3237625Freely accessible. PMID 21998196. 
  6. ^ Chhabra ES, Ramabhadran V, Gerber SA, Higgs HN (May 2009). "INF2 is an endoplasmic reticulum-associated formin protein". Journal of Cell Science. 122 (Pt 9): 1430–40. doi:10.1242/jcs.040691. PMC 2721004Freely accessible. PMID 19366733. 
  7. ^ a b Skau CT, Plotnikov SV, Doyle AD, Waterman CM (May 2015). "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): E2447–56. doi:10.1073/pnas.1505035112. PMC 4434736Freely accessible. PMID 25918420. 
  8. ^ Korobova F, Ramabhadran V, Higgs HN (January 2013). "An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2". Science. 339 (6118): 464–7. doi:10.1126/science.1228360. PMC 3843506Freely accessible. PMID 23349293. 
  9. ^ Gurel PS, Ge P, Grintsevich EE, Shu R, Blanchoin L, Zhou ZH, Reisler E, Higgs HN (January 2014). "INF2-mediated severing through actin filament encirclement and disruption". Current Biology. 24 (2): 156–64. doi:10.1016/j.cub.2013.12.018. PMC 3992431Freely accessible. PMID 24412206. 
  10. ^ Brown EJ, Schlöndorff JS, Becker DJ, Tsukaguchi H, Tonna SJ, Uscinski AL, Higgs HN, Henderson JM, Pollak MR (January 2010). "Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis". Nature Genetics. 42 (1): 72–6. doi:10.1038/ng.505. PMC 2980844Freely accessible. PMID 20023659. 
  11. ^ Boyer O, Nevo F, Plaisier E, Funalot B, Gribouval O, Benoit G, Huynh Cong E, Arrondel C, Tête MJ, Montjean R, Richard L, Karras A, Pouteil-Noble C, Balafrej L, Bonnardeaux A, Canaud G, Charasse C, Dantal J, Deschenes G, Deteix P, Dubourg O, Petiot P, Pouthier D, Leguern E, Guiochon-Mantel A, Broutin I, Gubler MC, Saunier S, Ronco P, Vallat JM, Alonso MA, Antignac C, Mollet G (December 2011). "INF2 mutations in Charcot-Marie-Tooth disease with glomerulopathy". The New England Journal of Medicine. 365 (25): 2377–88. doi:10.1056/NEJMoa1109122. PMID 22187985. 

Further reading[edit]