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Fermitin family member 1

kindlin-1, KIND1, FERMT1
This gene encodes a member of the fermitin family, and contains a FERM domain and a pleckstrin homology domain. The encoded protein is involved in integrin signaling and linkage of the actin cytoskeleton to the extracellular matrix. Mutations in this gene have been linked to Kindler syndrome. [provided by RefSeq, Dec 2009] (from NCBI)
Top mentioned proteins: MIG2, Actin, CAN, HAD, V1a
Papers on kindlin-1
The kindlin family: functions, signaling properties and implications for human disease.
Fässler et al., Martinsried, Germany. In J Cell Sci, Feb 2016
Mutations in the KINDLIN-1 (also known as FERMT1) gene cause Kindler syndrome (KS) - in which mainly skin and intestine are affected, whereas mutations in the KINDLIN-3 (also known as FERMT3) gene cause leukocyte adhesion deficiency type III (LAD III), which is characterized by impaired extravasation of blood effector cells and severe, spontaneous bleedings.
A novel large deletion mutation of FERMT1 gene in a Chinese patient with Kindler syndrome.
Song et al., Beijing, China. In J Zhejiang Univ Sci B, Nov 2015
The majority of mutations of the disease-determining gene (FERMT1 gene) are single nucleotide substitutions, including missense mutations, nonsense mutations, etc.
Full length talin stimulates integrin activation and axon regeneration.
Fawcett et al., Cambridge, United Kingdom. In Mol Cell Neurosci, Sep 2015
Overexpressing kindlin-1 in dorsal root ganglion (DRG) neurons activates integrins, enabling their axons to overcome inhibitory molecules in the environment, and promoting regeneration in vivo following dorsal root crush.
FERMT1 promoter mutations in patients with Kindler syndrome.
Castiglia et al., Freiburg, Germany. In Clin Genet, Sep 2015
Mutations in the FERMT1 gene, encoding the focal adhesion protein kindlin-1 underlie the Kindler syndrome (KS), an autosomal recessive skin disorder with a phenotype comprising skin blistering, photosensitivity, progressive poikiloderma with extensive skin atrophy, and propensity to skin cancer.
Lineage specific expression of Polycomb Group Proteins in human embryonic stem cells in vitro.
Bhartiya et al., Mumbai, India. In Cell Biol Int, May 2015
In-house derived hES cell line KIND1 was differentiated into endoderm, mesoderm, and ectoderm lineages; followed by characterization using RT-PCR for HNF4A, CDX2, MEF2C, TBX5, SOX1, and MAP2.
Site-specific phosphorylation of kindlin-3 protein regulates its capacity to control cellular responses mediated by integrin αIIbβ3.
Plow et al., Cleveland, United States. In J Biol Chem, Apr 2015
Thr(482) or Ser(484) was identified as a phosphorylation site, which resides in a sequence not conserved in kindlin-1 or kindlin-2.
Whole-exome sequencing improves mutation detection in a diagnostic epidermolysis bullosa laboratory.
McGrath et al., London, United Kingdom. In Br J Dermatol, 2015
RESULTS: Analysis of WES data disclosed biallelic pathogenic mutations in each case, with all mutations occurring in known EB genes (LAMB3, PLEC, FERMT1 and COL7A1).
Kindler syndrome with severe mucosal involvement in a large Palestinian pedigree.
Naim et al., Roma, Italy. In Eur J Dermatol, 2015
KS is caused by mutations in the FERMT1 gene encoding kindlin-1.
Genome Wide Methylome Alterations in Lung Cancer.
Spivack et al., New York City, United States. In Plos One, 2014
Of the canonical changes noted, promoter (PR) DM loci with reciprocal changes in expression in adenocarcinomas included HBEGF, AGER, PTPRM, DPT, CST1, MELK; DM GB loci with concordant changes in expression included FOXM1, FERMT1, SLC7A5, and FAP genes.
Integrins in periodontal disease.
Häkkinen et al., Vancouver, Canada. In Exp Cell Res, 2014
Patients with kindlin-1 mutations have severe early-onset periodontal disease.
Polycomb group protein expression during differentiation of human embryonic stem cells into pancreatic lineage in vitro.
Bhartiya et al., Mumbai, India. In Bmc Cell Biol, 2013
RESULTS: In-house derived hES cell line KIND1 was used to study expression of PcG protein upon spontaneous and directed differentiation towards pancreatic lineage.
Kindlin-3 in the immune system.
Morrison et al., Helsinki, Finland. In Am J Clin Exp Immunol, 2013
In contrast to kindlin-1 and kindlin-2 proteins, kindlin-3 is expressed mainly in the hematopoietic system.
Oxidative stress and mitochondrial dysfunction in Kindler syndrome.
Del Rio et al., Valencia, Spain. In Orphanet J Rare Dis, 2013
In spite of the knowledge underlying cause of this disease involving mutations of FERMT1 (fermitin family member 1), and efforts to characterize genotype-phenotype correlations, the clinical variability of this genodermatosis is still poorly understood.
Founder mutation c.676insC in three unrelated Kindler syndrome families belonging to a particular clan from Pakistan.
Raja et al., In J Dermatol, 2012
Direct sequencing of the FERMT1 gene revealed a homozygous insertion of cytosine at position 676 (c.676insC) in exon 5 in seven patients.
Kindler syndrome: extension of FERMT1 mutational spectrum and natural history.
Bruckner-Tuderman et al., Freiburg, Germany. In Hum Mutat, 2011
There is an association of FERMT1 missense and in-frame deletion mutations with milder disease phenotypes, and later onset of complications in Kindler syndrome ( FERMT1 )
Role of the focal adhesion protein kindlin-1 in breast cancer growth and lung metastasis.
Driouch et al., Saint-Cloud, France. In J Natl Cancer Inst, 2011
Kindlin-1 expression in breast tumors is associated with lung metastasis and lung metastasis-free survival through regulation of TGF-beta signaling. Kindlin-1-silencing prevented tumor growth and lung metastasis in mice.
Novel and recurrent FERMT1 gene mutations in Kindler syndrome.
Lai-Cheong et al., London, United Kingdom. In Acta Derm Venereol, 2011
Describe five novel and three recurrent loss-of-function FERMT1 mutations in eight individuals with Kindler syndrome, and provide an overview of genotype-phenotype correlation in this disorder.
Kindlin-1 and -2 have overlapping functions in epithelial cells implications for phenotype modification.
Has et al., Freiburg, Germany. In Am J Pathol, 2011
The phenotype of kindlin-1-deficient cells can be modulated by regulating kindlin-2 gene expression and vice versa.
Kindler syndrome.
McGrath et al., London, United Kingdom. In Dermatol Clin, 2010
Loss-of-function mutations in the FERMT1 gene are the cause of Kindler syndrome.
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