YPERMAN, K., Anna PAPAGEORGIOU, R. MERCERON, S. DE MUNCK, Y. BLOCH, D. EECKHOUT, Q.H. JIANG, P. TACK, R. GRIGORYAN, Thomas EVANGELIDIS, J. VAN LEENE, L. VINCZE, P. VANDENABEELE, F. VANHAECKE, M. POTOCKY, G. DE JAEGER, S.N. SAVVIDES, Konstantinos TRIPSIANES, R. PLESKOT and D. VAN DAMME. Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding. Nature Communications. London: Nature Publishing Group, 2021, vol. 12, No 1, p. "3050", 11 pp. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/s41467-021-23314-6.
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Basic information
Original name Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding
Authors YPERMAN, K., Anna PAPAGEORGIOU (300 Greece, belonging to the institution), R. MERCERON, S. DE MUNCK, Y. BLOCH, D. EECKHOUT, Q.H. JIANG, P. TACK, R. GRIGORYAN, Thomas EVANGELIDIS (300 Greece, belonging to the institution), J. VAN LEENE, L. VINCZE, P. VANDENABEELE, F. VANHAECKE, M. POTOCKY, G. DE JAEGER, S.N. SAVVIDES, Konstantinos TRIPSIANES (300 Greece, guarantor, belonging to the institution), R. PLESKOT and D. VAN DAMME.
Edition Nature Communications, London, Nature Publishing Group, 2021, 2041-1723.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 17.694
RIV identification code RIV/00216224:14740/21:00122020
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1038/s41467-021-23314-6
UT WoS 000658769900002
Keywords in English Adaptor Proteins; Signal Transducing; Calcium-Binding Proteins; Cell Membrane; X-Ray; NMR; Molecular Dynamics Simulation
Tags CF NMR, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 26/2/2022 13:18.
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. AtEH/Pan1 proteins contain two N-terminal Eps15 homology (EH) domains and are subunits of the endocytic TPLATE complex present in plants. Here, the authors combine X-ray crystallography, NMR and MD simulations with biochemical and in planta analysis to characterize the two AtEH1/Pan1 EH domains and reveal their structural differences and complementary functional roles.
Links
LM2018127, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
LQ1601, research and development projectName: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR
MUNI/G/0739/2017, interní kód MUName: Pushing the limits in automated NMR structure determination using a single 4D NOESY spectrum and machine learning methods
Investor: Masaryk University, INTERDISCIPLINARY - Interdisciplinary research projects
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