ArticleNature communications2021
Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Clathrin-Mediated Endocytosis in Plants: Historical to Modern Advances.Traffic (Copenhagen, Denmark) · 2026Review
- Plasma membrane invaginations and their diverse cellular functions.BMC biology · 2026Review
- Cell-type-specific gating of gene regulatory modules as a hallmark of early immune responses in Arabidopsis leaves.The New phytologist · 2026Article
- Implementing In Vitro and In Vivo Approaches to Analyze Lipid-Protein Interactions in Growing Tobacco Pollen Tubes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Nuclear Effector RIRG190 Interacts with SAS10 to Regulate Arbuscular Mycorrhizal Symbiosis.International journal of molecular sciences · 2025Article
- A combined biochemical and computational approach provides evidence for membrane remodelling by the structural scaffold of the endocytic TPLATE complex.Nature plants · 2025Article
- Structural Insights and Calcium-Switching Mechanism ofInternational journal of molecular sciences · 2025Article
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- A developmentally controlled cellular decompartmentalization process executes programmed cell death in the Arabidopsis root cap.The Plant cell · 2024Article
- Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants.Nature cell biology · 2024Article
- Exploring the potential role of fourFrontiers in plant science · 2024Article
- TPLATE complex-dependent endocytosis attenuates CLAVATA1 signaling for shoot apical meristem maintenance.EMBO reports · 2023Article
- The endocytic TPLATE complex internalizes ubiquitinated plasma membrane cargo.Nature plants · 2022Article
- TheeLife · 2022Article
- Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components.The Plant 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
- Phosphatidic Acid in Plant Hormonal Signaling: From Target Proteins to Membrane Conformations.International journal of molecular sciences · 2022Review
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- Constitutive Active CPK30 Interferes With Root Growth and Endomembrane Trafficking inFrontiers in plant science · 2022Article
- The TPLATE complex mediates membrane bending during plant clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
20 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clathrin-mediated endocytosis (CME) is the gatekeeper of the plasma membrane. In contrast to animals and yeasts, CME in plants depends on the TPLATE complex (TPC), an evolutionary ancient adaptor complex. However, the mechanistic contribution of the individual TPC subunits to plant CME remains elusive. In this study, we used a multidisciplinary approach to elucidate the structural and functional roles of the evolutionary conserved N-terminal Eps15 homology (EH) domains of the TPC subunit AtEH1/Pan1. By integrating high-resolution structural information obtained by X-ray crystallography and NMR spectroscopy with all-atom molecular dynamics simulations, we provide structural insight into the function of both EH domains. Both domains bind phosphatidic acid with a different strength, and only the second domain binds phosphatidylinositol 4,5-bisphosphate. Unbiased peptidome profiling by mass-spectrometry revealed that the first EH domain preferentially interacts with the double N-terminal NPF motif of a previously unidentified TPC interactor, the integral membrane protein Secretory Carrier Membrane Protein 5 (SCAMP5). Furthermore, we show that AtEH/Pan1 proteins control the internalization of SCAMP5 via this double NPF peptide interaction motif. Collectively, our structural and functional studies reveal distinct but complementary roles of the EH domains of AtEH/Pan1 in plant CME and connect the internalization of SCAMP5 to the TPLATE complex.
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