Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2022 Jan;49(1):735-746.
doi: 10.1007/s11033-021-06869-x. Epub 2021 Oct 26.

Role of formin INF2 in human diseases

Yiting Zhao  1   2 , Hui Zhang  3   2 , Haibiao Wang  4   5 , Meng Ye  6   7 , Xiaofeng Jin  8   9
Affiliations
Review

Role of formin INF2 in human diseases

Yiting Zhao et al. Mol Biol Rep. 2022 Jan.

Abstract

Formin proteins catalyze actin nucleation and microfilament polymerization. Inverted formin 2 (INF2) is an atypical diaphanous-related formin characterized by polymerization and depolymerization of actin. Accumulating evidence showed that INF2 is associated with kidney disease focal segmental glomerulosclerosis and cancers, such as colorectal and thyroid cancer where it functions as a tumor suppressor, glioblastoma, breast, prostate, and gastric cancer, via its oncogenic function. However, studies on the underlying molecular mechanisms of the different roles of INF2 in diverse cancers are limited. This review comprehensively describes the structure, biochemical features, and primary pathogenic mutations of INF2.

Keywords: CMT; Cancers; FSGS; Formin; INF2; Mutations.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Woychik RP, Maas RL, Zeller R, Vogt TF, Leder P (1990) “Formins”: proteins deduced from the alternative transcripts of the limb deformity gene. Nature 346:850–853. https://doi.org/10.1038/346850a0 - DOI - PubMed
    1. Chen Q, Nag S, Pollard TD (2012) Formins filter modified actin subunits during processive elongation. J Struct Biol 177:32–39. https://doi.org/10.1016/j.jsb.2011.10.005 - DOI - PubMed
    1. Romero S, Le Clainche C, Didry D, Egile C, Pantaloni D, Carlier MF (2004) Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119:419–429. https://doi.org/10.1016/j.cell.2004.09.039 - DOI - PubMed
    1. Bartolini F, Gundersen GG (2010) Formins and microtubules. Biochim Biophys Acta 1803:164–173. https://doi.org/10.1016/j.bbamcr.2009.07.006 - DOI - PubMed
    1. Breitsprecher D, Goode BL (2013) Formins at a glance. J Cell Sci 126:1–7. https://doi.org/10.1242/jcs.107250 - DOI - PubMed - PMC

LinkOut - more resources