Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding

Klaas Yperman, Anna C. Papageorgiou, Romain Merceron, Steven De Munck, Yehudi Bloch, Dominique Eeckhout, Qihang Jiang, Pieter Tack, Rosa Grigoryan, Thomas Evangelidis, Jelle Van Leene, Laszlo Vincze, Peter Vandenabeele, Frank Vanhaecke, Martin Potocký, Geert De Jaeger, Savvas N. Savvides (), Konstantinos Tripsianes (), Roman Pleskot () and Daniel Van Damme ()
Additional contact information
Klaas Yperman: Ghent University
Anna C. Papageorgiou: Masaryk University
Romain Merceron: Ghent University
Steven De Munck: Ghent University
Yehudi Bloch: Ghent University
Dominique Eeckhout: Ghent University
Qihang Jiang: Ghent University
Pieter Tack: Ghent University
Rosa Grigoryan: Ghent University
Thomas Evangelidis: Masaryk University
Jelle Van Leene: Ghent University
Laszlo Vincze: Ghent University
Peter Vandenabeele: Ghent University
Frank Vanhaecke: Ghent University
Martin Potocký: Academy of Sciences of the Czech Republic
Geert De Jaeger: Ghent University
Savvas N. Savvides: Ghent University
Konstantinos Tripsianes: Masaryk University
Roman Pleskot: Ghent University
Daniel Van Damme: Ghent University

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23314-6

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DOI: 10.1038/s41467-021-23314-6

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