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Formin 2

Fmn2, formin-2
Formin homology (FH) domain proteins (see FMN1; MIM 136535) play a role in cytoskeletal organization and/or establishment of cell polarity.[supplied by OMIM, Apr 2010] (from NCBI)
Top mentioned proteins: Actin, DAAM1, DAAM2, ACID, FRL
Papers on Fmn2
Formin-2 regulates stabilization of filopodial tip adhesions in growth cones and affects neuronal outgrowth and pathfinding in vivo.
Ghose et al., Pune, India. In Development, Jan 2016
However, little is known about the influence of filopodial actin structures on substrate adhesion and filopodial contractility.Formin-2 (Fmn2) localizes along filopodial actin bundles and its depletion does not affect filopodia initiation or elongation.
Role of the C-terminal extension of Formin 2 in its activation by Spire and processive assembly of actin filaments.
Carlier et al., France. In J Biol Chem, Jan 2016
UNASSIGNED: Formin 2 (Fmn2), a member of the FMN family of formins, plays an important role in early development.
The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells.
Walz et al., Freiburg, Germany. In J Cell Biol, Jan 2016
Knockdown of daam1, but not formin-2, resulted in similar disruption of the subapical actin web, whereas nphp4 depletion prevented the association of Inturned with the basal bodies.
Genomic regulation of senescence and innate immunity signaling in the retinal pigment epithelium.
Bhattacharya et al., Memphis, United States. In Mamm Genome, Jun 2015
Many of the genes in this QTL locus are involved in innate immune responses, including Fc receptors, interferon-inducible family genes, and formin 2. Importantly, we found an age-related increase in FCGR3A and FMN2 and a decrease in IFI16 levels in RPE cultures.
Mechanical stimulation induces formin-dependent assembly of a perinuclear actin rim.
Shivashankar et al., Singapore, Singapore. In Proc Natl Acad Sci U S A, Jun 2015
However, the endoplasmic reticulum- and nuclear membrane-associated inverted formin-2 (INF2), a potent actin polymerization activator (mutations of which are associated with several genetic diseases), was found to be important for perinuclear actin assembly.
Membrane targeting of the Spir·formin actin nucleator complex requires a sequential handshake of polar interactions.
Kerkhoff et al., Dresden, Germany. In J Biol Chem, Apr 2015
Interestingly, we found that the intramolecular Spir-2 FYVE/KIND and the trans-regulatory Fmn-2-FSI/Spir-2-KIND interactions are competitive.
Biallelic truncating mutations in FMN2, encoding the actin-regulatory protein Formin 2, cause nonsyndromic autosomal-recessive intellectual disability.
Gleeson et al., Toronto, Canada. In Am J Hum Genet, 2015
Using a combination of homozygosity mapping and next-generation sequencing in two consanguineous families affected by nonsyndromic autosomal-recessive intellectual disability, we identified truncating mutations in formin 2 (FMN2), encoding a protein that belongs to the formin family of actin cytoskeleton nucleation factors and is highly expressed in the maturing brain.
Genome-wide copy number analysis in a family with p.G533C RET mutation and medullary thyroid carcinoma identified regions potentially associated with a higher predisposition to lymph node metastasis.
Cerutti et al., São Paulo, Brazil. In J Clin Endocrinol Metab, 2014
The validation step confirmed that a CNV loss impacting the FMN2 gene was potentially associated with a greater predisposition to lymph node metastasis in this family (P = .0179).
Identification of GPM6A and GPM6B as potential new human lymphoid leukemia-associated oncogenes.
Rassart et al., Montréal, Canada. In Cell Oncol (dordr), 2014
We observed over-expression of a variety of genes, including Arntl2, Bfsp2, Gfra2, Gpm6a, Gpm6b, Nln, Fbln1, Bmp7, Etv5 and Celsr1 and, in addition, provided evidence that Fmn2 and Parm-1 may act as novel oncogenes.
A novel INF2 mutation in a Korean family with autosomal dominant intermediate Charcot-Marie-Tooth disease and focal segmental glomerulosclerosis.
Choi et al., Seoul, South Korea. In J Peripher Nerv Syst, 2014
Mutations in the inverted formin-2 (INF2) gene were recently identified in patients with autosomal dominant intermediate Charcot-Marie-Tooth (DI-CMT) disease and focal segmental glomerulosclerosis (FSGS).
Spire and Formin 2 synergize and antagonize in regulating actin assembly in meiosis by a ping-pong mechanism.
Carlier et al., Gif-sur-Yvette, France. In Plos Biol, 2014
In mammalian oocytes, three actin binding proteins, Formin 2 (Fmn2), Spire, and profilin, synergistically organize a dynamic cytoplasmic actin meshwork that mediates translocation of the spindle toward the cortex and is required for successful fertilization.
Polarity gene alterations in pure invasive micropapillary carcinomas of the breast.
Vincent-Salomon et al., In Breast Cancer Res, 2013
Whole-exome sequencing combined with RNA sequencing of IMPC allowed us to identify somatic mutations in genes involved in polarity, DNAH9 and FMN2 (8% and 2%, respectively) or ciliogenesis, BBS12 and BBS9 (2% each) or genes coding for endoplasmic reticulum protein, HSP90B1 and SPTLC3 (2% each) and cytoskeleton, UBR4 and PTPN21 (2% each), regardless of the genomic subset.
Symmetry breaking and polarity establishment during mouse oocyte maturation.
Li et al., Kansas City, United States. In Philos Trans R Soc Lond B Biol Sci, 2012
This feedback loop not only maintains meiotic II spindle position during metaphase II arrest, but also brings about symmetry breaking during meiosis I. Prior to an Arp2/3-dependent phase of fast movement, meiotic I spindle experiences a slow and non-directional first phase of migration driven by a pushing force from Fmn2-mediated actin polymerization.
Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)•formin-2 formin SPIR interaction motif (FSI) complex.
Kerkhoff et al., Tübingen, Germany. In J Biol Chem, 2011
analysis of the molecular basis of the Spir1/formin-2 interaction
Symmetry breaking in mouse oocytes requires transient F-actin meshwork destabilization.
Verlhac et al., Paris, France. In Development, 2011
High formin 2 levels at meiosis I entry induce meshwork maintenance, leading to equal forces being exerted on the chromosomes, preventing spindle migration.
Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division.
Schuh et al., Cambridge, United Kingdom. In Curr Biol, 2011
Spire1 and Spire2 cooperate with Formin-2 (Fmn2) to nucleate actin filaments in mouse oocytes.
Gene profiling of Graffi murine leukemia virus-induced lymphoid leukemias: identification of leukemia markers and Fmn2 as a potential oncogene.
Rassart et al., Montréal, Canada. In Blood, 2011
Gene profiling of Fmn2 in Graffi murine leukemia virus-induced lymphoid leukemias suggest its important role in leukemogenesis.
Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins.
Kerkhoff et al., Regensburg, Germany. In J Biol Chem, 2009
both mammalian Spir proteins, Spir-1 and Spir-2, interact with mammalian Fmn subgroup proteins formin-1 and formin-2
Actin-driven chromosomal motility leads to symmetry breaking in mammalian meiotic oocytes.
Li et al., Kansas City, United States. In Nat Cell Biol, 2008
Formation of these filaments depends on the actin nucleation activity of Fmn2, a formin-family protein that concentrates around chromosomes through its amino-terminal region.
Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle in mouse oocytes.
Leder et al., Boston, United States. In Nat Cell Biol, 2002
formin-2 is a maternal-effect gene that is expressed in oocytes and is required for progression through metaphase of meiosis I
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