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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

MIG2 Mig2p

MIG2, kindlin-2, kindlin-3, Mig2p, UNC-112
Top mentioned proteins: Akt, CAN, Actin, kindlin-1, HAD
Papers on MIG2
Kindlin-2 promotes invasiveness of prostate cancer cells via NF-κB-dependent upregulation of matrix metalloproteinases.
Qian et al., Wuhan, China. In Gene, Feb 2016
In this study, we aimed to investigate the role of kindlin-2, an integrin-binding focal adhesion protein, in the regulation of invasiveness of prostate cancer.
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.
Kindlin-2 siRNA inhibits vascular smooth muscle cell proliferation, migration and intimal hyperplasia via Wnt signaling.
Li et al., Wuhan, China. In Int J Mol Med, Jan 2016
In the present study, we investigated the effects of kindlin-2 on VSMC proliferation, migration and intimal hyperplasia, and the underlying mechanisms.
In vivo adhesion of malignant B cells to bone marrow microvasculature is regulated by α4β1 cytoplasmic-binding proteins.
Teixidó et al., Madrid, Spain. In Leukemia, Jan 2016
Talin, kindlin-3 and ICAP-1 are β1-integrin-binding partners that regulate β1-mediated cell adhesion.
Exposure to the lampricide 3-trifluoromethyl-4-nitrophenol results in increased expression of carbohydrate transporters in S. cerevisiae.
Olsen et al., Norwich, United Kingdom. In Environ Toxicol Chem, Dec 2015
Among the most significantly up regulated genes were regulators of carbohydrate transport including HXT1, HXT3, HXT4, IMA5, MIG2, and YKR075C.
Regulation of integrins in platelets.
Bennett, Philadelphia, United States. In Biopolymers, Jul 2015
Second, the agonist-stimulated binding of the cytosolic proteins talin and kindlin-3 to the β3 cytosolic tail rapidly causes αIIbβ3 activation by disrupting the intramolecular interactions constraining αIIbβ3 activity.
Kindlin-3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells.
Tan et al., Singapore, Singapore. In Sci Rep, 2014
Kindlin-3 is expressed in hematopoietic cells, platelets, and endothelial cells.
An approach for exploring interaction between two proteins in vivo.
Benian et al., Atlanta, United States. In Front Physiol, 2013
We describe our experience using this strategy to study the interaction of UNC-112 (kindlin) with PAT-4 (integrin linked kinase).
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.
The molecular basis of leukocyte recruitment and its deficiencies.
Sperandio et al., München, Germany. In Mol Immunol, 2013
Finally, LAD-III, also known as LAD-I variant, is caused by impaired integrin activation due to mutations within the kindlin-3 gene.
Kindlin 2 forms a transcriptional complex with β-catenin and TCF4 to enhance Wnt signalling.
Zhang et al., Beijing, China. In Embo Rep, 2012
Kindlin 2 forms a tripartite complex with beta-catenin and TCF4.
Spatial coordination of kindlin-2 with talin head domain in interaction with integrin β cytoplasmic tails.
Plow et al., Cleveland, United States. In J Biol Chem, 2012
Kindlin-2 and talin head do not interact with one another but can bind simultaneously to the integrin beta(3) tail without enhancing or inhibiting the interaction of the other binding partner.
Kindlin-3 mediates integrin αLβ2 outside-in signaling, and it interacts with scaffold protein receptor for activated-C kinase 1 (RACK1).
Tan et al., Singapore, Singapore. In J Biol Chem, 2012
integrin alphaLbeta2 engagement by its ligand ICAM-1 promotes the association of kindlin-3 with RACK1
Nodal proteins are target antigens in Guillain-Barré syndrome.
Yuki et al., Saint-Pierre-des-Corps, France. In J Peripher Nerv Syst, 2012
gliomedin, NF186, and contactin are novel target antigens in Guillain-Barre syndrome
Interactive effects of ATOH7 and RFTN1 in association with adult-onset primary open-angle glaucoma.
Zhang et al., Shantou, China. In Invest Ophthalmol Vis Sci, 2012
combination of ATOH7 and RFTN1 SNPs increased risk to POAG, indicating their diversified effects in the complex genetics of glaucoma.
Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation.
Hogg et al., London, United Kingdom. In Nat Med, 2009
identify mutations in the KINDLIN3 (official symbol FERMT3) gene specifying the KINDLIN-3 protein as the cause of leukocyte adhesion deficiency-III in Maltese and Turkish subjects
A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans.
Byzova et al., Cleveland, United States. In Nat Med, 2009
The genetic basis for this disease was traced to a point mutation in the coding region of the KINDLIN3 (official gene symbol FERMT3) gene.
SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function.
Mann et al., Martinsried, Germany. In Cell, 2008
SILAC analysis from various organs lacking expression of beta1 integrin, beta-Parvin, or the integrin tail-binding protein Kindlin-3 confirmed their absence and disclosed a structural defect of the red blood cell membrane skeleton in Kindlin-3-deficient erythrocytes.
Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation.
Wu et al., Pittsburgh, United States. In Cell, 2003
Migfilin interacts with the cell-matrix adhesion protein Mig-2 (mitogen inducible gene-2), a mammalian homolog of UNC-112, and the actin binding protein filamin through its C- and N-terminal domains, respectively.
Role of a new Rho family member in cell migration and axon guidance in C. elegans.
Kenyon et al., San Francisco, United States. In Cell, 1997
Our findings support this conclusion and show that mig-2 functions redundantly with another pathway to regulate nuclear migration.
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