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EHD1, EHD2, and EHD4 are recruited to caveolae. Recruitment of the other EHDs increases markedly when EHD2, which has been previously detected at caveolae, is absent. Construction of knockout cell lines lacking EHDs 1, 2, and 4 confirms this apparent functional redundancy.
These findings reveal a novel and functionally important role for EHD1 in governing CSF-1R signalling via regulation of anterograde transport of CSF-1R to the macrophage cell surface.
regulates the maintenance of T-tubules through its interaction with BIN1
these data reveal a unique role for EHD1 in early lens development.
Early steps in primary cilium assembly require EHD1/EHD3-dependent ciliary vesicle formation.
tubule formation in myoblasts relies on a functional EHD1 ATPase domain. EHD1 regulates BIN1 induced tubule formation.
The characterization of Fer1L5 and its interaction with EHD1 and EHD2 underscores the complex requirement of ferlin proteins and mediators of endocytic recycling for membrane trafficking events during myotube formation
Histopathology revealed abnormal spermatogenesis in the seminiferous tubules and the absence of mature spermatozoa in the epididymides of Ehd1-/- males.
EHD3: a protein that resides in recycling tubular and vesicular membrane structures and interacts with EHD1.
EHD1 and EHBP1, but not EHD2, are required for perinuclear localization of GLUT4 and reveal that loss of EHBP1 disrupts insulin-regulated GLUT4 recycling in cultured adipocytes.
EHD1 may regulate/participate in the functional pathways of both GS32 and syndapin II in a mutual exclusive manner
ATP binding is required for oligomerization of mRme-1/EHD1, which in turn is required for its association with endosomes
Data support a role for EHD1 in beta1 integrin recycling, and demonstrate a requirement for EHD1 in integrin-mediated downstream functions.
PACSIN1 and EHD1 assemble membrane tubules from the developing intracellular cilium that attach to the plasma membrane, creating an extracellular membrane channel to the outside of the cell.
Depletion of myosin-Va significantly inhibits the attachment of preciliary vesicles to the distal appendages of the mother centriole and decreases cilia assembly. Myosin-Va functions upstream of EHD1- and Rab11-mediated ciliary vesicle formation.
Results suggest that EHD1 is a cisplatin (CDDP)-resistant gene that suppresses DNA adduct-induced apoptosis by modulating intracellular CDDP concentrations.
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
RAB11FIP3 combines with Eps15 homology domain 1 to promote the endocytosis recycling of phosphorylation of epithelial growth factor receptor.
van der Waals interactions should be the main consideration when we design peptide inhibitors of EHD1 EH domain with high affinities.
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.
that Molecule Interacting with CasL Like-1 and Eps15 Homology Domain protein 1 differentially influence microtubule dynamics during early and late mitosis
Transport through recycling endosomes requires EHD1 recruitment by a phosphatidylserine translocase.
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).
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.
evidence that the functions of both EHD1 and EHD4 are primarily in TRE membrane vesiculation, whereas EHD3 is a membrane-tubulating protein.
the lipid modifier cPLA2alpha and EHD1 are involved in the vesiculation of CD59-containing endosomes
Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function
EHD1 is involved in the control of CD59 transport from pre-sorting endosomes to the ERC in a PKC-dependent manner
A new class of cardiac trafficking proteins(EHD1, EHD2, EHD3, EHD4) regulates cardiac membrane protein targeting.
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.
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.
A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane
This gene belongs to a highly conserved gene family encoding EPS15 homology (EH) domain-containing proteins. The protein-binding EH domain was first noted in EPS15, a substrate for the epidermal growth factor receptor. The EH domain has been shown to be an important motif in proteins involved in protein-protein interactions and in intracellular sorting. The protein encoded by this gene is thought to play a role in the endocytosis of IGF1 receptors.
EH domain-containing protein 1
, PAST homolog 1
, EH-domain containing 1
, EH-domain containing 3, like
, EH-domain-containing protein 1
, EH-domain containing 1a