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Role of Formin INF2 in Human Diseases

Overview
Journal Mol Biol Rep
Specialty Molecular Biology
Date 2021 Oct 26
PMID 34698992
Citations 10
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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.

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References
1.
Woychik R, Maas R, Zeller R, Vogt T, Leder P . 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene. Nature. 1990; 346(6287):850-3. DOI: 10.1038/346850a0. View

2.
Chen Q, Nag S, Pollard T . Formins filter modified actin subunits during processive elongation. J Struct Biol. 2011; 177(1):32-9. PMC: 3683246. DOI: 10.1016/j.jsb.2011.10.005. View

3.
Romero S, Clainche C, Didry D, Egile C, Pantaloni D, Carlier M . Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell. 2004; 119(3):419-29. DOI: 10.1016/j.cell.2004.09.039. View

4.
Bartolini F, Gundersen G . Formins and microtubules. Biochim Biophys Acta. 2009; 1803(2):164-73. PMC: 2856479. DOI: 10.1016/j.bbamcr.2009.07.006. View

5.
Breitsprecher D, Goode B . Formins at a glance. J Cell Sci. 2013; 126(Pt 1):1-7. PMC: 3603506. DOI: 10.1242/jcs.107250. View