A broadly conserved NERD genetically interacts with the exocyst to affect root growth and cell expansion

The exocyst, a conserved, octameric protein complex, helps mediate secretion at the plasma membrane, facilitating specific developmental processes that include control of root meristem size, cell elongation, and tip growth. A genetic screen for second-site enhancers in Arabidopsis identified NEW ENH...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 69(2018), 15 vom: 27. Juni, Seite 3625-3637
1. Verfasser: Cole, Rex A (VerfasserIn)
Weitere Verfasser: Peremyslov, Valera V, Van Why, Savannah, Moussaoui, Ibrahim, Ketter, Ann, Cool, Renee, Moreno, Matthew Andres, Vejlupkova, Zuzana, Dolja, Valerian V, Fowler, John E
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S. AT3G51050 protein, Arabidopsis Arabidopsis Proteins Nuclear Proteins Polysaccharides Recombinant Fusion Proteins Green Fluorescent Proteins 147336-22-9
Beschreibung
Zusammenfassung:The exocyst, a conserved, octameric protein complex, helps mediate secretion at the plasma membrane, facilitating specific developmental processes that include control of root meristem size, cell elongation, and tip growth. A genetic screen for second-site enhancers in Arabidopsis identified NEW ENHANCER of ROOT DWARFISM1 (NERD1) as an exocyst interactor. Mutations in NERD1 combined with weak exocyst mutations in SEC8 and EXO70A1 result in a synergistic reduction in root growth. Alone, nerd1 alleles modestly reduce primary root growth, both by shortening the root meristem and by reducing cell elongation, but also result in a slight increase in root hair length, bulging, and rupture. NERD1 was identified molecularly as At3g51050, which encodes a transmembrane protein of unknown function that is broadly conserved throughout the Archaeplastida. A functional NERD1-GFP fusion localizes to the Golgi, in a pattern distinct from the plasma membrane-localized exocyst, arguing against a direct NERD1-exocyst interaction. Structural modeling suggests the majority of the protein is positioned in the lumen, in a β-propeller-like structure that has some similarity to proteins that bind polysaccharides. We suggest that NERD1 interacts with the exocyst indirectly, possibly affecting polysaccharides destined for the cell wall, and influencing cell wall characteristics in a developmentally distinct manner
Beschreibung:Date Completed 17.10.2019
Date Revised 17.10.2019
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/ery162