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

J 2021

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

YPERMAN, K.; Anna PAPAGEORGIOU; R. MERCERON; S. DE MUNCK; Y. BLOCH et al.

Základní údaje

Originální název

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

Autoři

Vydání

Nature Communications, London, Nature Publishing Group, 2021, 2041-1723

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 17.694

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/21:00122020

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Adaptor Proteins; Signal Transducing; Calcium-Binding Proteins; Cell Membrane; X-Ray; NMR; Molecular Dynamics Simulation

Štítky

CF NMR, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 15. 10. 2024 14:21, Ing. Jana Kuchtová

Anotace

V originále

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.

Návaznosti

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

MUNI/G/0739/2017, interní kód MU

Název: Pushing the limits in automated NMR structure determination using a single 4D NOESY spectrum and machine learning methods

Investor: Masarykova univerzita, Pushing the limits in automated NMR structure determination using a single 4D NOESY spectrum and machine learning methods, INTERDISCIPLINARY - Mezioborové výzkumné projekty

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

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 a D. VAN DAMME. Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding. Nature Communications. London: Nature Publishing Group, 2021, roč. 12, č. 1, s. "3050", 11 s. ISSN 2041-1723. Dostupné z: https://doi.org/10.1038/s41467-021-23314-6.

@article{1784537,
   author = {Yperman, K. and Papageorgiou, Anna and Merceron, R. and De Munck, S. and Bloch, Y. and Eeckhout, D. and Jiang, Q.H. and Tack, P. and Grigoryan, R. and Evangelidis, Thomas and Van Leene, J. and Vincze, L. and Vandenabeele, P. and Vanhaecke, F. and Potocky, M. and De Jaeger, G. and Savvides, S.N. and Tripsianes, Konstantinos and Pleskot, R. and Van Damme, D.},
   article_location = {London},
   article_number = {1},
   doi = {https://doi.org/10.1038/s41467-021-23314-6},
   keywords = {Adaptor Proteins; Signal Transducing; Calcium-Binding Proteins; Cell Membrane; X-Ray; NMR; Molecular Dynamics Simulation},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding},
   url = {https://www.ncbi.nlm.nih.gov/pubmed/34031427},
   volume = {12},
   year = {2021}
}

TY  - JOUR
ID  - 1784537
AU  - Yperman, K. - Papageorgiou, Anna - Merceron, R. - De Munck, S. - Bloch, Y. - Eeckhout, D. - Jiang, Q.H. - Tack, P. - Grigoryan, R. - Evangelidis, Thomas - Van Leene, J. - Vincze, L. - Vandenabeele, P. - Vanhaecke, F. - Potocky, M. - De Jaeger, G. - Savvides, S.N. - Tripsianes, Konstantinos - Pleskot, R. - Van Damme, D.
PY  - 2021
TI  - Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding
JF  - Nature Communications
VL  - 12
IS  - 1
SP  - "3050"
EP  - "3050"
PB  - Nature Publishing Group
SN  - 20411723
KW  - Adaptor Proteins
KW  - Signal Transducing
KW  - Calcium-Binding Proteins
KW  - Cell Membrane
KW  - X-Ray
KW  - NMR
KW  - Molecular Dynamics Simulation
UR  - https://www.ncbi.nlm.nih.gov/pubmed/34031427
N2  - 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.
ER  -

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 a D. VAN DAMME. Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding. \textit{Nature Communications}. London: Nature Publishing Group, 2021, roč.~12, č.~1, s.~''3050'', 11 s. ISSN~2041-1723. Dostupné z: https://doi.org/10.1038/s41467-021-23314-6.

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