Literature DB >> 34698992

Role of formin INF2 in human diseases.

Yiting Zhao1,2, Hui Zhang3,2, Haibiao Wang4,5, Meng Ye6,7, Xiaofeng Jin8,9.   

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.
© 2021. The Author(s), under exclusive licence to Springer Nature B.V.

Entities:  

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

Mesh:

Substances:

Year:  2021        PMID: 34698992     DOI: 10.1007/s11033-021-06869-x

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.316


  93 in total

1.  Mechanism of formin-induced nucleation of actin filaments.

Authors:  Martin Pring; Marie Evangelista; Charles Boone; Changsong Yang; Sally H Zigmond
Journal:  Biochemistry       Date:  2003-01-21       Impact factor: 3.162

2.  Determinants of Formin Homology 1 (FH1) domain function in actin filament elongation by formins.

Authors:  Naomi Courtemanche; Thomas D Pollard
Journal:  J Biol Chem       Date:  2012-01-14       Impact factor: 5.157

3.  Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain.

Authors:  Takanori Otomo; Diana R Tomchick; Chinatsu Otomo; Sanjay C Panchal; Mischa Machius; Michael K Rosen
Journal:  Nature       Date:  2005-01-05       Impact factor: 49.962

4.  Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis.

Authors:  Stéphane Romero; Christophe Le Clainche; Dominique Didry; Coumaran Egile; Dominique Pantaloni; Marie-France Carlier
Journal:  Cell       Date:  2004-10-29       Impact factor: 41.582

5.  'Formins': proteins deduced from the alternative transcripts of the limb deformity gene.

Authors:  R P Woychik; R L Maas; R Zeller; T F Vogt; P Leder
Journal:  Nature       Date:  1990-08-30       Impact factor: 49.962

Review 6.  Formins and microtubules.

Authors:  F Bartolini; G G Gundersen
Journal:  Biochim Biophys Acta       Date:  2009-07-23

Review 7.  Formins at a glance.

Authors:  Dennis Breitsprecher; Bruce L Goode
Journal:  J Cell Sci       Date:  2013-01-01       Impact factor: 5.285

8.  Formins filter modified actin subunits during processive elongation.

Authors:  Qian Chen; Shalini Nag; Thomas D Pollard
Journal:  J Struct Biol       Date:  2011-10-25       Impact factor: 2.867

Review 9.  Actin, a central player in cell shape and movement.

Authors:  Thomas D Pollard; John A Cooper
Journal:  Science       Date:  2009-11-27       Impact factor: 47.728

10.  The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation.

Authors:  Aditya S Paul; Aditya Paul; Thomas D Pollard; Thomas Pollard
Journal:  Curr Biol       Date:  2007-12-20       Impact factor: 10.834

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  1 in total

1.  DDX17 modulates the expression and alternative splicing of genes involved in apoptosis and proliferation in lung adenocarcinoma cells.

Authors:  Cheng He; Gan Zhang; Yanhong Lu; Jingyue Zhou; Zixue Ren
Journal:  PeerJ       Date:  2022-09-21       Impact factor: 3.061

  1 in total

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