Sphingolipid biosynthesis modulates plasmodesmal ultrastructure and phloem unloading.
Arabidopsis
/ genetics
Arabidopsis Proteins
/ genetics
Genes, Plant
Glucans
/ metabolism
Green Fluorescent Proteins
/ metabolism
Membrane Proteins
/ genetics
Mutation
Phloem
/ metabolism
Plant Roots
/ metabolism
Plasmodesmata
/ metabolism
Sphingolipids
/ biosynthesis
Transferases (Other Substituted Phosphate Groups)
/ genetics
Journal
Nature plants
ISSN: 2055-0278
Titre abrégé: Nat Plants
Pays: England
ID NLM: 101651677
Informations de publication
Date de publication:
06 2019
06 2019
Historique:
received:
03
09
2018
accepted:
17
04
2019
pmc-release:
10
12
2019
entrez:
12
6
2019
pubmed:
12
6
2019
medline:
28
8
2019
Statut:
ppublish
Résumé
During phloem unloading, multiple cell-to-cell transport events move organic substances to the root meristem. Although the primary unloading event from the sieve elements to the phloem pole pericycle has been characterized to some extent, little is known about post-sieve element unloading. Here, we report a novel gene, PHLOEM UNLOADING MODULATOR (PLM), in the absence of which plasmodesmata-mediated symplastic transport through the phloem pole pericycle-endodermis interface is specifically enhanced. Increased unloading is attributable to a defect in the formation of the endoplasmic reticulum-plasma membrane tethers during plasmodesmal morphogenesis, resulting in the majority of pores lacking a visible cytoplasmic sleeve. PLM encodes a putative enzyme required for the biosynthesis of sphingolipids with very-long-chain fatty acid. Taken together, our results indicate that post-sieve element unloading involves sphingolipid metabolism, which affects plasmodesmal ultrastructure. They also raise the question of how and why plasmodesmata with no cytoplasmic sleeve facilitate molecular trafficking.
Identifiants
pubmed: 31182845
doi: 10.1038/s41477-019-0429-5
pii: 10.1038/s41477-019-0429-5
pmc: PMC6565433
mid: EMS82696
doi:
Substances chimiques
Arabidopsis Proteins
0
At1g43580 protein, Arabidopsis
0
Glucans
0
Membrane Proteins
0
Sphingolipids
0
Green Fluorescent Proteins
147336-22-9
callose
9064-51-1
Transferases (Other Substituted Phosphate Groups)
EC 2.7.8.-
phosphatidylcholine-ceramide phosphocholine transferase
EC 2.7.8.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
604-615Subventions
Organisme : European Research Council
ID : 323052
Pays : International
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/N013158/1
Pays : United Kingdom
Commentaires et corrections
Type : CommentIn
Type : ErratumIn
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