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Epsin and Sla2 form assemblies through phospholipid interfaces

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Epsin and Sla2 form assemblies through phospholipid interfaces. / Garcia-Alai, Maria M; Heidemann, Johannes; Skruzny, Michal; Gieras, Anna; Mertens, Haydyn D T; Svergun, Dmitri I; Kaksonen, Marko; Uetrecht, Charlotte; Meijers, Rob.

in: NAT COMMUN, Jahrgang 9, Nr. 1, 23.01.2018, S. 328.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Garcia-Alai, MM, Heidemann, J, Skruzny, M, Gieras, A, Mertens, HDT, Svergun, DI, Kaksonen, M, Uetrecht, C & Meijers, R 2018, 'Epsin and Sla2 form assemblies through phospholipid interfaces', NAT COMMUN, Jg. 9, Nr. 1, S. 328. https://doi.org/10.1038/s41467-017-02443-x

APA

Garcia-Alai, M. M., Heidemann, J., Skruzny, M., Gieras, A., Mertens, H. D. T., Svergun, D. I., Kaksonen, M., Uetrecht, C., & Meijers, R. (2018). Epsin and Sla2 form assemblies through phospholipid interfaces. NAT COMMUN, 9(1), 328. https://doi.org/10.1038/s41467-017-02443-x

Vancouver

Garcia-Alai MM, Heidemann J, Skruzny M, Gieras A, Mertens HDT, Svergun DI et al. Epsin and Sla2 form assemblies through phospholipid interfaces. NAT COMMUN. 2018 Jan 23;9(1):328. https://doi.org/10.1038/s41467-017-02443-x

Bibtex

@article{e502a4fb99eb4580a706c555ab4d27cc,
title = "Epsin and Sla2 form assemblies through phospholipid interfaces",
abstract = "In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.",
keywords = "Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Binding Sites, Cell Membrane, Chaetomium, Crystallography, X-Ray, Endocytosis, Fungal Proteins, Humans, Models, Molecular, Phosphatidylinositol 4,5-Diphosphate, Protein Binding, Protein Domains, Protein Multimerization, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Journal Article, Research Support, Non-U.S. Gov't",
author = "Garcia-Alai, {Maria M} and Johannes Heidemann and Michal Skruzny and Anna Gieras and Mertens, {Haydyn D T} and Svergun, {Dmitri I} and Marko Kaksonen and Charlotte Uetrecht and Rob Meijers",
year = "2018",
month = jan,
day = "23",
doi = "10.1038/s41467-017-02443-x",
language = "English",
volume = "9",
pages = "328",
journal = "NAT COMMUN",
issn = "2041-1723",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - Epsin and Sla2 form assemblies through phospholipid interfaces

AU - Garcia-Alai, Maria M

AU - Heidemann, Johannes

AU - Skruzny, Michal

AU - Gieras, Anna

AU - Mertens, Haydyn D T

AU - Svergun, Dmitri I

AU - Kaksonen, Marko

AU - Uetrecht, Charlotte

AU - Meijers, Rob

PY - 2018/1/23

Y1 - 2018/1/23

N2 - In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.

AB - In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.

KW - Adaptor Proteins, Vesicular Transport

KW - Amino Acid Sequence

KW - Binding Sites

KW - Cell Membrane

KW - Chaetomium

KW - Crystallography, X-Ray

KW - Endocytosis

KW - Fungal Proteins

KW - Humans

KW - Models, Molecular

KW - Phosphatidylinositol 4,5-Diphosphate

KW - Protein Binding

KW - Protein Domains

KW - Protein Multimerization

KW - Saccharomyces cerevisiae

KW - Sequence Homology, Amino Acid

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/s41467-017-02443-x

DO - 10.1038/s41467-017-02443-x

M3 - SCORING: Journal article

C2 - 29362354

VL - 9

SP - 328

JO - NAT COMMUN

JF - NAT COMMUN

SN - 2041-1723

IS - 1

ER -