PI4P and BLOC-1 remodel endosomal membranes into tubules

Riddhi Atul Jani, Aurélie Di Cicco, Tal Keren-Kaplan, Silvia Vale-Costa, Daniel Hamaoui, Ilse Hurbain, Feng-Ching Tsai, Mathilde Dimarco, Anne-Sophie Macé, Yueyao Zhu, Maria João Amorim, Patricia Bassereau, Juan Bonifacino, Agathe Subtil, Michael Marks, Daniel Lévy*, Graça Raposo, Cédric Delevoye*

*Autor correspondente para este trabalho

Resultado de pesquisarevisão de pares

1 Citação (Scopus)

Resumo

Intracellular trafficking is mediated by transport carriers that originate by membrane remodeling from donor organelles. Tubular carriers contribute to the flux of membrane lipids and proteins to acceptor organelles, but how lipids and proteins impose a tubular geometry on the carriers is incompletely understood. Using imaging approaches on cells and in vitro membrane systems, we show that phosphatidylinositol-4-phosphate (PI4P) and biogenesis of lysosome-related organelles complex 1 (BLOC-1) govern the formation, stability, and functions of recycling endosomal tubules. In vitro, BLOC-1 binds and tubulates negatively charged membranes, including those containing PI4P. In cells, endosomal PI4P production by type II PI4-kinases is needed to form and stabilize BLOC-1-dependent recycling endosomal tubules. Decreased PI4KIIs expression impairs the recycling of endosomal cargoes and the life cycles of intracellular pathogens such as Chlamydia bacteria and influenza virus that exploit the membrane dynamics of recycling endosomes. This study demonstrates how a phospholipid and a protein complex coordinate the remodeling of cellular membranes into functional tubules.

Idioma originalEnglish
Número do artigoe202110132
RevistaJournal of Cell Biology
Volume221
Número de emissão11
DOIs
Estado da publicaçãoPublicado - 7 nov 2022

Impressão digital

Mergulhe nos tópicos de investigação de “PI4P and BLOC-1 remodel endosomal membranes into tubules“. Em conjunto formam uma impressão digital única.

Citação