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EHD2 encodes a member of the EH domain-containing protein family. Additionally we are shipping EHD2 Antibodies (36) and many more products for this protein.
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Data suggest that the EH-domain containing 2 protein (EHD2) NPF phenylalanine residue is crucial for EHD2 localization to the plasma membrane, whereas the proline residue is essential for EHD2 dimerization and binding.
EHD2 can inhibit the metastasis of human breast cancer by regulating the epithelial-to-mesenchymal transition markers E-cadherin (show CDH1 Proteins) and N-cadherin (show CDH2 Proteins).
Downregulation of EHD2 was associated with migration and invasion by abrogating the expression of Rac1 in breast cancer patients.
Phosphatidylinositol 4,5-bisphosphate controls EHD2 plasma membrane localization.
Our results suggested that EHD2 low expression is involved in the pathogenesis of human esophageal squamous cell carcinoma
EHD2 participates in the sarcolemma repair.
Assembly of EHD2 stabilized and constrained caveolae to the plasma membrane to control turnover, and depletion of EHD2, resulting in endocytic and more dynamic and short-lived caveolae.
Among three EHD proteins (EHD1-EHD3 (show EHD3 Proteins)) that were tested, only EHD2 accumulates in the nucleus under nuclear export inhibition treatment.
Confining caveolae to the plasma membrane by EHD2 relied on its capacity to link caveolae to actin filaments.
EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity.
The helical domain of EHD2 (show EHD3 Proteins) is inserted into the membrane.The N terminus domain regulates caveolar targeting of EHD2 (show EHD3 Proteins).
Assembly of EHD2 (show EHD3 Proteins) stabilized and constrained caveolae to the plasma membrane to control turnover, and depletion of EHD2 (show EHD3 Proteins), resulting in endocytic and more dynamic and short-lived caveolae.
The characterization of Fer1L5 and its interaction with EHD1 (show EHD1 Proteins) and EHD2 (show EHD3 Proteins) underscores the complex requirement of ferlin proteins and mediators of endocytic recycling for membrane trafficking events during myotube formation
appears to connect endocytosis to the actin cytoskeleton through interactions of its N-terminal domain with membranes and its C-terminal EH domain with the novel EHBP1 protein
interaction of myoferlin with EHD2 (show EHD3 Proteins) identifies molecular overlap between the endocytic recycling pathway and the machinery that regulates myoblast membrane fusion
This gene encodes a member of the EH domain-containing protein family. These proteins are characterized by a C-terminal EF-hand domain, a nucleotide-binding consensus site at the N terminus and a bipartite nuclear localization signal. The encoded protein interacts with the actin cytoskeleton through an N-terminal domain and also binds to an EH domain-binding protein through the C-terminal EH domain. This interaction appears to connect clathrin-dependent endocytosis to actin, suggesting that this gene product participates in the endocytic pathway.
EH-domain containing 2
, EH domain-containing protein 2
, EH-domain containing 1
, EH-domain-containing protein 2
, EH domain-containing protein 2-like
, EH domain containing 2
, PAST homolog 2
, putative eps protein