FMNL3

Formin-like protein 3 (FMNL3), also known as WW domain-binding protein 3 (WBP-3), is a protein that in humans is encoded by the FMNL3 gene.{{cite web | title = Entrez Gene: formin-like 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=91010| accessdate = }}{{cite journal | vauthors = Katoh M, Katoh M | title = Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes in silico | journal = International Journal of Oncology | volume = 22 | issue = 5 | pages = 1161–8 | date = May 2003 | pmid = 12684686 | doi = 10.3892/ijo.22.5.1161 }}

Function

The protein encoded by this gene contains a formin homology 2 domain and has high sequence identity to the mouse Wbp3 protein. Two alternative transcripts encoding different isoforms have been described. The C-terminus has been shown to accelerate actin polymerization activity of this protein through its WH2-like motif.{{cite journal | vauthors = Heimsath EG, Higgs HN | title = The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends | journal = The Journal of Biological Chemistry | volume = 287 | issue = 5 | pages = 3087–98 | date = Jan 2012 | pmc = 3270965 | doi = 10.1074/jbc.M111.312207 | pmid = 22094460 | doi-access = free }} FMNL3 has been crystallized in complex with actin providing insight into the mechanism of formin-mediated actin nucleation.{{cite journal | vauthors = Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ | title = FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation | journal = Nature Structural & Molecular Biology | volume = 20 | issue = 1 | pages = 111–8 | date = Jan 2013 | pmid = 23222643 | pmc = 3876896 | doi = 10.1038/nsmb.2462 }}

FMNL3

Function

See also

References

Further reading