EHD3 Protein Is Required for Tubular Recycling Endosome Stabilization, and an Asparagine-Glutamic Acid Residue Pair within Its Eps15 Homology (EH) Domain Dictates Its Selective Binding to NPF Peptides
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Title
EHD3 Protein Is Required for Tubular Recycling Endosome Stabilization, and an Asparagine-Glutamic Acid Residue Pair within Its Eps15 Homology (EH) Domain Dictates Its Selective Binding to NPF Peptides
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 26, Pages 13465-13478
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2016-05-05
DOI
10.1074/jbc.m116.716407
References
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Note: Only part of the references are listed.- Phosphatidic acid induces EHD3-containing membrane tubulation and is required for receptor recycling
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- SUMOylation of EHD3 Modulates Tubulation of the Endocytic Recycling Compartment
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- Diacylglycerol Kinase α Regulates Tubular Recycling Endosome Biogenesis and Major Histocompatibility Complex Class I Recycling
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- Rabankyrin-5 Interacts with EHD1 and Vps26 to Regulate Endocytic Trafficking and Retromer Function
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- Eps15 Homology Domain 1-associated Tubules Contain Phosphatidylinositol-4-Phosphate and Phosphatidylinositol-(4,5)-Bisphosphate and Are Required for Efficient Recycling
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- (2009) Barth D. Grant et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1
- (2009) Fabien Kieken et al. PROTEIN SCIENCE
- 5-Fluoro-2-indolyl des-chlorohalopemide (FIPI), a Phospholipase D Pharmacological Inhibitor That Alters Cell Spreading and Inhibits Chemotaxis
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