How phosphoinositides shape autophagy in plant cells.

Arabidopsis Proteins / metabolism Autophagy / physiology Endosomes / metabolism Phosphatidylinositol Phosphates / metabolism Phosphatidylinositols / metabolism Plant Cells / metabolism Vesicular Transport Proteins / metabolism
Autophagosome Endosome Phosphatidylinositol 3-kinase VPS38

Journal

Plant science : an international journal of experimental plant biology
ISSN: 1873-2259
Titre abrégé: Plant Sci
Pays: Ireland
ID NLM: 9882015

Informations de publication

Date de publication:
Apr 2019
Historique:
received: 05 09 2018
revised: 10 01 2019
accepted: 19 01 2019
entrez: 3 3 2019
pubmed: 3 3 2019
medline: 19 3 2019
Statut: ppublish

Résumé

Plant cells use autophagy to degrade their own cytoplasm in vacuoles, thereby not only recycling their breakdown products, but also ensuring the homeostasis of essential cytoplasmic constituents and organelles. Plants and other eukaryotes have a conserved set of core Autophagy-related (ATG) genes involved in the biogenesis of the autophagosome, the main autophagic compartment destined for the lytic vacuole. In the past decade, the core ATG genes were isolated from several plant species. The core ATG proteins include the components of the VACUOLAR PROTEIN SORTING 34 (VPS34) complex that is responsible for the local production of phosphatidylinositol 3-phosphate (PI3P) at the site of autophagosome formation. Dissecting the roles of PI3P and its effectors in autophagy is challenging, because of the multi-faceted links between autophagosomal and endosomal systems. This review highlights recent studies on putative plant PI3P effectors involved in autophagosome dynamics. Molecular mechanisms underlying the requirement of PI3P for autophagosome biogenesis and trafficking are also discussed.

Identifiants

DOI: 10.1016/j.plantsci.2019.01.017 PMID: 30824047
pubmed: 30824047
pii: S0168-9452(18)31101-4
doi: 10.1016/j.plantsci.2019.01.017
pii:
doi:

Substances chimiques

Arabidopsis Proteins 0
Phosphatidylinositol Phosphates 0
Phosphatidylinositols 0
VPS38 protein, Arabidopsis 0
Vesicular Transport Proteins 0
phosphatidylinositol 3-phosphate 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

146-158

Informations de copyright

Copyright © 2019 Elsevier B.V. All rights reserved.

Auteurs

Taijoon Chung (T)

Department of Biological Sciences, Pusan National University, Busan, 46241, Republic of Korea. Electronic address: taijoon@pusan.ac.kr.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines végétales › Protéines d'Arabidopsis › How phosphoinositides shape autophagy in plant cells.
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Autophagie › How phosphoinositides shape autophagy in plant cells.
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Vésicules cytoplasmiques › Vésicules de transport › Endosomes › How phosphoinositides shape autophagy in plant cells.
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Glycérophosphate › Acides phosphatidiques › Glycérophospholipides › Phosphatidyl inositols › Phosphates phosphatidylinositol › How phosphoinositides shape autophagy in plant cells.
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Glycérophosphate › Acides phosphatidiques › Glycérophospholipides › Phosphatidyl inositols › How phosphoinositides shape autophagy in plant cells.
questionsmedicales.fr › Cellules › Cellules végétales › How phosphoinositides shape autophagy in plant cells.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines du transport vésiculaire › How phosphoinositides shape autophagy in plant cells.