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Twinfilin, actin-binding protein, homolog 1

A-6, twinfilin
This gene encodes twinfilin, an actin monomer-binding protein conserved from yeast to mammals. Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures may be regulated by the small GTPase RAC1. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Actin, cofilin, twinfilin-2, gelsolin, Drebrin
Papers on A-6
A twinfilin-like protein coordinates karyokinesis by influencing mitotic spindle elongation and DNA replication in Leishmania.
Sahasrabuddhe et al., Lucknow, India. In Mol Microbiol, Jan 2016
UNASSIGNED: Twinfilin is an evolutionarily conserved actin-binding protein, which regulates actin-dynamics in eukaryotic cells.
Combinatorial genetic analysis of a network of actin disassembly-promoting factors.
Goode et al., Waltham, United States. In Cytoskeleton (hoboken), Jul 2015
Saccharomyces cerevisiae is an ideal system to tackle this problem, both because of its amenabilities to genetic manipulation and live-cell imaging and because only a single gene encodes each of the core disassembly factors: cofilin (COF1), Srv2/CAP (SRV2), Aip1 (AIP1), GMF (GMF1/AIM7), coronin (CRN1), and twinfilin (TWF1).
Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe.
Aligue et al., Barcelona, Spain. In Plos One, 2014
We show that inhibition of Cdc25 by Srk1 is regulated by Ssp1; and also that restoring growth polarity and actin localization of ssp1-deleted cells by removing the actin-monomer-binding protein, twinfilin, is sufficient to suppress the ssp1 phenotype.
Verification of a Parkinson's disease protein signature in T-lymphocytes by multiple reaction monitoring.
Fasano et al., Busto Arsizio, Italy. In J Proteome Res, 2014
A similar result is achieved by evaluating all peptides of a selected panel of proteins (gelsolin, moesin, septin-6, twinfilin-2, lymphocyte-specific protein 1, vimentin, transaldolase), with an area under the curve of 0.840.
Breaking limitations of complex culture media: functional non-viral miRNA delivery into pharmaceutical production cell lines.
Otte et al., Biberach an der Riß, Germany. In J Biotechnol, 2013
We provide evidence for the functionality of transferred ncRNAs by demonstrating siRNA-mediated changes in protein levels and cellular phenotype as well as decreased twinfilin-1 (twf-1) transcript levels by its upstream miR-1 regulator.
Elements of functional genital asymmetry in the cow.
Gómez et al., Gijón, Spain. In Reprod Fertil Dev, 2013
Among 60 uterine proteins identified by difference gel electrophoresis, relative abundance of nine (acyl-CoA dehydrogenase, very long chain; twinfilin, actin-binding protein, homologue 1; enolase 1; pyruvate kinase isozymes M1/M2 (rabbit); complement factor B Bb fragment ; albumin; fibrinogen gamma-B chain; and ezrin differed (P<0.05) between horns.
Effects of actin-binding proteins on the thermal stability of monomeric actin.
Levitsky et al., Moscow, Russia. In Biochemistry, 2013
Differential scanning calorimetry (DSC) was applied to investigate the thermal unfolding of rabbit skeletal muscle G-actin in its complexes with actin-binding proteins, cofilin, twinfilin, and profilin.
MicroRNA-30c targets cytoskeleton genes involved in breast cancer cell invasion.
Liu et al., Chicago, United States. In Breast Cancer Res Treat, 2013
Here, we show that human breast tumor biomarker miR-30c regulates invasion by targeting the cytoskeleton network genes encoding twinfilin 1 (TWF1) and vimentin (VIM).
MicroRNA-30c inhibits human breast tumour chemotherapy resistance by regulating TWF1 and IL-11.
Liu et al., Chicago, United States. In Nat Commun, 2012
Here we report that microRNA-30c, a human breast tumour prognostic marker, has a pivotal role in chemoresistance by a direct targeting of the actin-binding protein twinfilin 1, which promotes epithelial-to-mesenchymal transition.
Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics.
Lappalainen et al., Helsinki, Finland. In Cytoskeleton (hoboken), 2011
ADF/cofilin promotes disassembly of aged actin filaments, whereas twinfilin inhibits actin filament assembly via sequestering actin monomers and interacting with filament barbed ends.
Twinfilin-2a is dispensable for mouse development.
Lappalainen et al., Helsinki, Finland. In Plos One, 2010
Mammals express three twinfilin isoforms, of which twinfilin-1 and twinfilin-2a display largely overlapping expression patterns in non-muscle tissues of developing and adult mice.
Attenuation of microRNA-1 derepresses the cytoskeleton regulatory protein twinfilin-1 to provoke cardiac hypertrophy.
Jing et al., Shanghai, China. In J Cell Sci, 2010
protein overexpression promotes cardiomyocyte hypertrophy
Drosophila twinfilin is required for cell migration and synaptic endocytosis.
Zhang et al., Beijing, China. In J Cell Sci, 2010
Twinfilin promotes actin turnover in multiple cellular processes that are highly dependent on actin dynamics.
In vivo RNAi screening identifies regulators of actin dynamics as key determinants of lymphoma progression.
Hemann et al., Cambridge, United States. In Nat Genet, 2009
Additionally, suppression of two of these targets, Rac2 and twinfilin, potentiated the action of the front-line chemotherapeutic vincristine, suggesting a critical relationship between cell motility and tumor relapse in hematopoietic malignancies.
Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse Twf2 gene by alternative promoter usage.
Lappalainen et al., Helsinki, Finland. In Biochem J, 2009
like Twf1, mouse Twf2 is a filament barbed-end capping protein, and that two tissue-specific and biochemically distinct isoforms are generated from the Twf2 gene through alternative promoter usage
Structure of the actin-depolymerizing factor homology domain in complex with actin.
Lappalainen et al., Helsinki, Finland. In J Cell Biol, 2008
The crystal structure of twinfilin's C-terminal ADF-H domain in complex with an actin monomer, is presented.
Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo.
Goode et al., Waltham, United States. In J Cell Sci, 2006
Together, our data suggest that twinfilin coordinates filament severing and monomer sequestering at sites of rapid actin turnover and is controlled by multiple regulatory inputs.
Regulation of cytoskeletal dynamics by actin-monomer-binding proteins.
Lappalainen et al., Helsinki, Finland. In Trends Cell Biol, 2004
In this article, we focus on recent advances in understanding how the six evolutionarily conserved actin-monomer-binding proteins - profilin, ADF/cofilin, twinfilin, Srv2/CAP, WASP/WAVE and verprolin/WIP - interact with actin monomers and regulate their incorporation into filament ends.
Twinfilin, a molecular mailman for actin monomers.
Lappalainen et al., Helsinki, Finland. In J Cell Sci, 2002
Twinfilin is a ubiquitous actin-monomer-binding protein that is composed of two ADF-homology domains.
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