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Novel kindlin-2 signaling axis that senses the mechanical cues of cell microenvironment and controls mesenchymal stem cell fate decision through YAP1/TAZ.
In a mouse model of wound healing, KINDLIN-2 gene knockdown inhibited wound healing, and increased neovascular permeability in vivo.
Our studies identify Kindlin-2 as a stabilizing linker of endothelial AJs with the actin cytoskeleton, thereby re-enforcing the vascular barrier.
Kindlin-2 is a key protein that couples cell adhesion by activating integrins and the induction of membrane protrusions by activating Rac1 and supplying Rac1 with the Arp2/3 complex.
demonstration that Smurf1 acts as a brake for integrin activation by controlling Kindlin-2 protein levels, a new mechanism that permits precise modulation of integrin-mediated cellular functions
Postnatal loss of Kindlin-2 from cardiac myocytes leads to progressive heart failure.
Data indicate that Kindlin-2 not only maintains the cardiac structure but also is required for cardiac function.
These findings show that talin and kindlin cooperatively activate integrins leading to fibronectin binding and adhesion.
These studies uncover a previously unrecognized function for Kindlin-2 and a mechanism for regulation of the chondrocyte differentiation programme and chondrogenesis.
Taken together, our study suggests the suppressive roles of Kindlin-2 in the pathogenesis of colorectal carcinoma
Data suggest that kindlin-2 (Kind2/Fermt2) interacts with actin alpha 2 (Actn2) and integrin beta 1 (Itgb1) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 leads to dissociation of Actn2 and Itgb1.
beta3/kindlin-2 interaction promotes outside-in alphaVbeta3 signaling selectively, with biological consequences in vivo [kindlin-2]
kindlin-2 tyrosine phosphorylation and interaction with Src serve as a regulatable switch downstream of focal adhesion kinase in the integrin outside-in signaling circuit controlling cell migration and proliferation
kindlin-2, through activating Ras and the downstream ERK1/2 and Akt signaling pathways, plays an important role in regulating renal tubular epithelial-to-mesenchymal transition
C-terminal LIM domains of migfilin 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 dynamics.
kindlin-2 regulates trafficking of endothelial cell surface enzymes that control platelet responses and hemostasis.
Kindlin-2 mediates activation of TGF-beta/Smad signaling and renal fibrosis.
Kindlin has a role in regulating integrin alpha5beta1 surface expression.
Mediation of Rac1 activation by kindlin-2: an essential function in osteoblast adhesion, spreading, and proliferation
Endothelial cells derived from kindlin-2(+/-) mice had integrin expression levels similar to WT mice but reduced alphaVbeta3-dependent signaling, migration, adhesion, spreading, and tube formation.
The expression of Kindlin-2 is up-regulated in gallbladder cancer tissues and Kindlin-2 promoted the malignant phenotypes of gallbladder cancer cells partially by epithelial-mesenchymal transition.
overexpression of Kindlin-2 might be a risk factor for lymph node metastasis.
Data confirmed the relevance of FERMT2 for podocyte functions. Its loss resulted in pronounced formation of membrane blebbing indicating cell cortex destabilization through redistribution of actin filaments and increased actomyosin tension. These indicate a competition between ECM-adhesion and the cortical cytoskeleton for the coupling and transmission of actomyosin tension influencing podocyte morphology and function.
Using molecular modeling and molecular dynamics simulations, we show that Asp344, Asp352, and Thr356 in kindlin-2 and Arg243 and Arg334 in ILK kinase domain (KD) are important in kindlin-2/ILK complex formation. Mutations that disrupt these interactions abrogate kindlin-2 and ILK colocalization in HeLa cells.
Results found Kindlin-2 expression upregulated in hepatocellular carcinoma (HCC) tissues and cell lines and it correlates with aggressive clinicopathological features and poor prognosis. Mechanistically, Kindlin-2 promotes HCC invasion, metastasis and epithelial-mesenchymal transition through Wnt/beta-catenin signaling.
Kindlin-2 is mainly expressed in the cytoplasm and nuclei of fibroblasts in the Esophageal cancer (EC) stroma. Kindlin-2 is upregulated in ECs compared with normal esophageal tissues. Kindlin-2 is more prevalent in poorly differentiated tumors. Kindlin-2 is expressed higher in EC smoker patients than non-smoker patients. Patients with a family history of EC show lower Kindlin-2 expression.
Long noncoding RNA-ATB functions as a molecular sponge for miR-200b and Kindlin-2.
Kindlin-2 is up-regulated in glioma cells and acts as an oncogene. It is an independent risk factor for poor prognosis. The Kindlin-2/YB-1/beta-catenin complex promotes EGFR transcription and contributes to glioma progression. Kindlin-2 is a potential diagnostic and prognostic marker in glioma, and inhibition of Kindlin-2 may be a novel strategy for glioma treatment.
the rs17125944 polymorphism in FERMT2 gene might not be association with late-onset Alzheimer's disease in northern Han Chinese population
analysis of the Kindlin-2-RhoGDIalpha-Rac1 signaling axis that is critical for regulation of podocyte structure and function in vivo
Study found that FERMT2 (a beta3-integrin co-activator) was significantly associated with a variation in cerebrospinal fluid Abeta peptide levels in 2886 Alzheimer's disease cases.Under-expression of FERMT2 increases Abeta peptide production by raising levels of mature APP at the cell surface and facilitating its recycling
High kindlin 2 expression is associated with Breast Cancer.
Data suggest that the extreme C terminus of kindlin-2 is essential for interaction with and activation of integrin alphaIIBbeta3; these studies were conducted in macrophage cell line and erythroleukemia cell line.
We show a direct relationship between kindlin-1 abundance and UV-B induced apoptosis in keratinocytes, whereas kindlin-2 overexpression has no compensatory effect.
The F0 domain of K2 binds actin.
data indicate that kindlin-2 promotes the invasiveness of prostate cancer cells largely through NF-kappaB-dependent upregulation of MMP-9 and MMP-2
High kindlin-2 expression is associated with esophageal squamous cell carcinoma.
our findings suggested that Kindlin-2 was highly expressed in hepatocellular carcinoma tissues and was closely related to clinical progression. Kindlin-2 protein could be a potential biomarker for predicting poor prognosis of HCC patients after surgery.
findings suggest that Src, Kindlin-2 and Migfilin together constitute a positive feedback loop that controls Src activity and regulates integrin-mediated cellular func
Participates in the connection between ECM adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits migfilin (FBLP1) protein to cell-ECM focal adhesion sites (By similarity).
fermitin family homolog 2
, mitogen inducible 2
, pleckstrin homology domain containing, family C (with FERM domain) member 1
, pleckstrin homology domain-containing family C member 1
, PH domain-containing family C member 1
, kindlin 2
, mitogen inducible gene 2 protein
, mitogen-inducible gene 2 protein
, pleckstrin homology domain containing, family C member 1