A combined biochemical and computational approach provides evidence for membrane remodelling by the structural scaffold of the endocytic TPLATE complex

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F25%3A00642186" target="_blank" >RIV/61389030:_____/25:00642186 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/25:10509631

Výsledek na webu

<a href="https://doi.org/10.1038/s41477-025-02146-y" target="_blank" >https://doi.org/10.1038/s41477-025-02146-y</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41477-025-02146-y" target="_blank" >10.1038/s41477-025-02146-y</a>

Jazyk výsledku

angličtina

Název v původním jazyce

A combined biochemical and computational approach provides evidence for membrane remodelling by the structural scaffold of the endocytic TPLATE complex

Popis výsledku v původním jazyce

Eukaryotic cells maintain homeostasis of their outer membrane by controlled internalization of lipid and protein constituents via endocytosis. Endocytosis is evolutionary conserved and uses similarly folded domains. How these structural folds are combined into proteins and protein complexes, however, differs between eukaryotic kingdoms. The TPLATE complex (TPC) in plants is an evolutionary ancient protein module that combines several protein domains with a conserved role in endocytosis into a single octameric protein complex. Its molecular architecture, lipid-nucleated condensate formation and requirement for clathrin cage curvature revealed its function in endocytosis initiation in plants. Mechanistic understanding of how this complex drives membrane deformation during plant endocytosis is, however, lacking. Here we used an integrative structural approach to obtain a precise molecular structure of the TPC of Arabidopsis thaliana. In addition, our approach allowed visualizing the structural flexibility that hallmarks this enigmatic complex. We prove that the intrinsic structural flexibility is required for its functionality and membrane recruitment. The membrane-binding interface consists of several domains with differential lipid preferences. Finally, we demonstrate via molecular dynamics simulations that the crescent shape of the structured part of the complex is sufficient for membrane curvature generation. Our mechanistic insight, obtained by a combined biochemical and computational approach, shows that the structured part of the TPC likely contributes to the execution of plant endocytosis, which does not depend on cytoskeletal-based force generation.

Název v anglickém jazyce

A combined biochemical and computational approach provides evidence for membrane remodelling by the structural scaffold of the endocytic TPLATE complex

Popis výsledku anglicky

Eukaryotic cells maintain homeostasis of their outer membrane by controlled internalization of lipid and protein constituents via endocytosis. Endocytosis is evolutionary conserved and uses similarly folded domains. How these structural folds are combined into proteins and protein complexes, however, differs between eukaryotic kingdoms. The TPLATE complex (TPC) in plants is an evolutionary ancient protein module that combines several protein domains with a conserved role in endocytosis into a single octameric protein complex. Its molecular architecture, lipid-nucleated condensate formation and requirement for clathrin cage curvature revealed its function in endocytosis initiation in plants. Mechanistic understanding of how this complex drives membrane deformation during plant endocytosis is, however, lacking. Here we used an integrative structural approach to obtain a precise molecular structure of the TPC of Arabidopsis thaliana. In addition, our approach allowed visualizing the structural flexibility that hallmarks this enigmatic complex. We prove that the intrinsic structural flexibility is required for its functionality and membrane recruitment. The membrane-binding interface consists of several domains with differential lipid preferences. Finally, we demonstrate via molecular dynamics simulations that the crescent shape of the structured part of the complex is sufficient for membrane curvature generation. Our mechanistic insight, obtained by a combined biochemical and computational approach, shows that the structured part of the TPC likely contributes to the execution of plant endocytosis, which does not depend on cytoskeletal-based force generation.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

<a href="/cs/project/GM22-35680M" target="_blank" >GM22-35680M: 4D buněčná přepážka</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Nature Plants

ISSN

2055-026X

e-ISSN

2055-0278

Svazek periodika

11

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

14

Strana od-do

2423-2436

Kód UT WoS článku

001613196800001

EID výsledku v databázi Scopus

2-s2.0-105021499404