ArticleBiochemistry2010
Charge effects in the selection of NPF motifs by the EH domain of EHD1.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 27 citations in OpenAlex.
- A Quarter Century of EHD Protein Research: From Endosomal Recycling to Ciliopathies.Traffic (Copenhagen, Denmark) · 2026Review
- The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026Article
- EnCPdock: a web-interface for direct conjoint comparative analyses of complementarity and binding energetics in inter-protein associations.Journal of molecular modeling · 2023Article
- Coronin2A links actin-based endosomal processes to the EHD1 fission machinery.Molecular biology of the cell · 2022Article
- Completing the family of human Eps15 homology domains: Solution structure of the internal Eps15 homology domain of γ-synergin.Protein science : a publication of the Protein Society · 2022Article
- Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding.Nature communications · 2021Article
- Article
- Thioether-stapled macrocyclic inhibitors of the EH domain of EHD1.Bioorganic & medicinal chemistry · 2018Article
- Acquisition of Rab11 and Rab11-Fip2-A novel strategy for Chlamydia pneumoniae early survival.PLoS pathogens · 2017Article
- 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.The Journal of biological chemistry · 2016Article
- Molecular dynamics simulation of the interactions between EHD1 EH domain and multiple peptides.Journal of Zhejiang University. Science. B · 2015Article
- Endosome-based protein trafficking and Ca(2+) homeostasis in the heart.Frontiers in physiology · 2015Review
- Role of the EHD2 unstructured loop in dimerization, protein binding and subcellular localization.PloS one · 2015Article
- Structured cyclic peptides that bind the EH domain of EHD1.Biochemistry · 2014Article
- Scratching the surface: actin' and other roles for the C-terminal Eps15 homology domain protein, EHD2.Histology and histopathology · 2014Review
- Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis.Molecular biology of the cell · 2013Article
- Role of phosphatidylinositol 4,5-bisphosphate in regulating EHD2 plasma membrane localization.PloS one · 2013Article
- A snapshot of the physical and functional wiring of the Eps15 homology domain network in the nematode.PloS one · 2013Article
- EHDs meet the retromer: Complex regulation of retrograde transport.Cellular logistics · 2012Article
- Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function.Traffic (Copenhagen, Denmark) · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Eps15 homology (EH) domain is found in proteins associated with endocytosis and vesicle trafficking. EH domains bind to their target proteins through an asparagine-proline-phenylalanine (NPF) motif. We have measured the interaction energetics of the EH domain from EHD1 with peptides derived from two of its binding partners: Rabenosyn-5 (Ac-GPSLNPFDEED-NH(2)) and Rab11-Fip2 (Ac-YESTNPFTAK-NH(2)). Heteronuclear single quantum coherence (HSQC) spectroscopy shows that both peptides bind in the canonical binding pocket of EHD1 EH and induce identical structural changes, yet the affinity of the negatively charged Ac-GPSLNPFDEED-NH(2) (K(a) = 8 x 10(5) M(-1)) is tighter by 2 orders of magnitude. The thermodynamic profiles (DeltaG, DeltaH, DeltaS) were measured for both peptides as a function of temperature. The enthalpies of binding are essentially identical, and the difference in affinity is a consequence of the difference in entropic cost. Ac-GPSLNPFDEED-NH(2) binding is salt-dependent, demonstrating an electrostatic component to the interaction, whereas Ac-YESTNPFTAK-NH(2) binding is independent of salt. Successive replacement of acidic residues in Ac-GPSLNPFDEED-NH(2) with neutral residues showed that all are important. Lysine side chains in EHD1 EH create a region of strong positive surface potential near the NPF binding pocket. Contributions by lysine epsilon-amino groups to complex formation with Ac-GPSLNPFDEED-NH(2) was shown using direct-observe (15)N NMR spectroscopy. These experiments have enabled us to define a new extended interaction motif for EHD proteins, N-P-F-[DE]-[DE]-[DE], which we have used to predict new interaction partners and hence broaden the range of cellular activities involving the EHD proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.