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FERMT1 encodes a member of the fermitin family, and contains a FERM domain and a pleckstrin homology domain. Additionally we are shipping FERMT1 Antibodies (48) and FERMT1 Kits (3) and many more products for this protein.
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The rof/kindlin-1 mutant zebrafish provi (show ILK Proteins)des a unique model system to study epidermal adhesion mechanisms in vivo.
Kindlin-1 is highly expressed in epithelial tissues derived from ectoderm and endoderm. Kindlin-1 was als (show FERMT2 Proteins)o found highly expressed in endoderm/ectoderm-derived tissues in embryos.
Kindlin-1 controls keratinocyte adhesion through beta1-class integrins and proliferation and differentiation of cutaneous epithelial stem cells via TGF-beta (show TGFB1 Proteins) activation and Wnt (show WNT2 Proteins)-beta-catenin (show CTNNB1 Proteins) signal inhibition.
Kindlin-1 and Kindlin-2 (show FERMT2 Proteins) have opposite roles in lung cancers
Kindlin-1 in mice gives rise to skin atrophy and an intestinal epithelial dysfunction with similarities to human ulcerative colitis.
Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
we show that a certain number of KS patients may harbor FERMT1 transcriptional regulatory mutations which are not routinely detected.
Kindlin-1 is highly expressed in epithelial tissues derived from ectoderm and endoderm, whereas Kindlin-2 (show FERMT2 Proteins) is mainly expressed in mesoderm-derived tissues. Likewise, Kindlin-1 was also found highly expressed in endoderm/ectoderm-derived tissues in embryos.
FERMT1 mutation causing Kindler syndrome.
our data suggest that Kindlin-1 could play an important role in hepatocellular carcinoma and might serve as a promising prognostic marker and potential target for hepatocellular carcinoma therapy.
A spectrum of FERMT1 mutations in 13 Iranian families with a diagnosis of Kindler syndrome have been ascertained.
We identified a novel mutation in FERMT1. These data are in agreement with the fact that the majority of KS-causing mutations in FERMT1 lead to premature termination of translation and to loss of kindlin-1 function in Kindler sysndrome
C-terminal LIM (show PDLIM5 Proteins) domains of migfilin (show FBLIM1 Proteins) dictate its focal adhesion localization, and these domains mediate an interaction with kindlin in vitro and in cells, demonstrating that kindlin is important for normal migfilin (show FBLIM1 Proteins) dynamics.
Data uncover a role for kindlin-1 in the regulation of integrin trafficking and adhesion turnover.
Short interfering RNA-mediated depletion of Kindlin-1 increases formation of abnormal mitotic spindles which is dependent on the ability of Kindlin-1 to bind integrins and Polo-like kinase 1-mediated Kindlin-1 phosphorylation.
Individuals with Kindler syndrome (KS) have loss-of-function mutations in the FERMT1 gene
Kindlin1 knockdown resulted in developmental delays, gross malformations of the gut (show GUSB Proteins) and eventual lethality by tadpole stages.
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.
fermitin family member 1
, fermitin family homolog 1
, fermitin family homolog 1-like
, unc-112-related protein 1
, UNC112 related protein 1
, kindlin 1
, kindlin syndrome protein
, UNC-112 related protein 1