An evolutionarily conserved motif is required for Plasmodesmata-located protein 5 to regulate cell-to-cell movement.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
05 06 2020
05 06 2020
Historique:
received:
22
05
2019
accepted:
04
05
2020
entrez:
7
6
2020
pubmed:
7
6
2020
medline:
16
6
2021
Statut:
epublish
Résumé
Numerous cell surface receptors and receptor-like proteins (RLPs) undergo activation or deactivation via a transmembrane domain (TMD). A subset of plant RLPs distinctively localizes to the plasma membrane-lined pores called plasmodesmata. Those RLPs include the Arabidopsis thaliana Plasmodesmata-located protein (PDLP) 5, which is well known for its vital function regulating plasmodesmal gating and molecular movement between cells. In this study, we report that the TMD, although not a determining factor for the plasmodesmal targeting, serves essential roles for the PDLP5 function. In addition to its role for membrane anchoring, the TMD mediates PDLP5 self-interaction and carries an evolutionarily conserved motif that is essential for PDLP5 to regulate cell-to-cell movement. Computational modeling-based analyses suggest that PDLP TMDs have high propensities to dimerize. We discuss how a specific mode(s) of TMD dimerization might serve as a common mechanism for PDLP5 and other PDLP members to regulate cell-to-cell movement.
Identifiants
pubmed: 32504045
doi: 10.1038/s42003-020-1007-0
pii: 10.1038/s42003-020-1007-0
pmc: PMC7275062
doi:
Substances chimiques
Arabidopsis Proteins
0
Membrane Proteins
0
PDLP5 protein, Arabidopsis
0
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
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