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Results suggest that EHD1 is a cisplatin (CDDP)-resistant gene that suppresses DNA adduct-induced apoptosis by modulating intracellular CDDP concentrations.
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this study shows that overexpression of EHD1 induced the epithelial-mesenchymal transition and increased the metastatic potential of lung cancer cells in vitro and in vivo
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RAB11FIP3 combines with Eps15 homology domain 1 to promote the endocytosis recycling of phosphorylation of epithelial growth factor receptor.
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van der Waals interactions should be the main consideration when we design peptide inhibitors of EHD1 EH domain with high affinities.
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Authors found that Eps15-homology domain 1 (EHD1), a protein that associates with the endocytic recycling compartment (ERC), colocalizes with active R-Ras in transiently expressed HeLa cells.
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that Molecule Interacting with CasL Like-1 and Eps15 Homology Domain protein 1 differentially influence microtubule dynamics during early and late mitosis
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Transport through recycling endosomes requires EHD1 recruitment by a phosphatidylserine translocase.
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Data indicate that concordant transforming growth factor-beta1 (TGFbeta-1) positive and EH-domain containing 1 (EHD1) negative as a strong favorable prognosis factor in non-small cell lung cancer (NSCLC).
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MICAL-L1-mediated recruitment of EHD1 to Src-containing recycling endosomes is required for the release of Src from the perinuclear endocytic recycling compartment in response to growth factor stimulation.
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evidence that the functions of both EHD1 and EHD4 are primarily in TRE membrane vesiculation, whereas EHD3 is a membrane-tubulating protein.
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the lipid modifier cPLA2alpha and EHD1 are involved in the vesiculation of CD59-containing endosomes
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Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function
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EHD1 is involved in the control of CD59 transport from pre-sorting endosomes to the ERC in a PKC-dependent manner
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A new class of cardiac trafficking proteins(EHD1, EHD2, EHD3, EHD4) regulates cardiac membrane protein targeting.
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The results indicate that NPF is the preferred binding motif for the EHD1 EH-domain, but both the DPF and GPF motifs are capable of binding with lower affinity.
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These data implicate MICAL-L1 as an unusual type of Rab effector that regulates endocytic recycling by recruiting and linking EHD1 and Rab8a on membrane tubules.
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A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane
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EHD3: a protein that resides in recycling tubular and vesicular membrane structures and interacts with EHD1.
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a novel interacting partner for EHD1, rabenosyn-5, was revealed.
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ATP binding is required for oligomerization of mRme-1/EHD1, which in turn is required for its association with endosomes
