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Our prognostic model is useful for predicting persistent/recurrent disease after surgery of Papillary thyroid carcinoma (PTC (show F9 Proteins)). EHD2 mRNA expression could be a novel prognostic marker for PTC (show F9 Proteins) patients.
EHD2 expression, along with the epithelial marker E-cadherin (show CDH1 Proteins), was markedly reduced in tumor tissues than in adjacent noncancerous tissues. Molecular data indicated that EHD2 inhibited migration and invasion of hepatocellular carcinoma probably by interacting with E-cadherin (show CDH1 Proteins).
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.
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