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demonstration that Smurf1 (show SMURF1 Proteins) 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 (show FN1 Proteins) 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 (show ACTN2 Proteins)) and integrin beta 1 (Itgb1 (show ITGB1 Proteins)) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 leads to dissociation of Actn2 (show ACTN2 Proteins) and Itgb1 (show ITGB1 Proteins).
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 (show AKT1 Proteins) signaling pathways, plays an important role in regulating renal tubular epithelial-to-mesenchymal transition
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 (show FERMT1 Proteins) 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 (show NFKB1 Proteins)-dependent upregulation of MMP-9 (show MMP9 Proteins) and MMP-2 (show MMP2 Proteins)
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 (show FAM126A Proteins) patients after surgery.
findings suggest that Src (show SRC Proteins), Kindlin-2 and Migfilin (show FBLIM1 Proteins) together constitute a positive feedback loop that controls Src (show SRC Proteins) activity and regulates integrin-mediated cellular func
Data indicate that Kindlin-2 mRNA levels in adult is highly expressed in mesoderm-derived organs.
A major ILK (show ILK Proteins) binding site in the kindlin-2 FERM domain for regulating cell adhesion has been mapped.
the first evidence that interaction between the integrin beta1 cytoplasmic tail and kindlin-2, a member of a family of adapters implicated in human disease pathogenesis, is mainly governed by the beta1 C-terminal carboxylate moiety
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