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Short Communication

Dual localization of the carboxy-terminal tail of GLR3.3 in sieve element–companion cell complex

ORCID Icon, & ORCID Icon
Article: 2167558 | Received 19 Dec 2022, Accepted 09 Jan 2023, Published online: 22 Jan 2023

References

  • Traynelis SF, Wollmuth LP, McBain CJ, et al. Glutamate receptor ion channels: structure, regulation, and function. Pharmacol Rev. 2010;62:405–4.
  • Lacombe B, Becker D, Hedrich R, et al. The identity of plant glutamate receptors. Science. 2001;292:1486–1487.
  • Grenzi M, Bonza MC, Costa A. Signaling by plant glutamate receptor-like channels: what else! Curr Opin Plant Biol. 2022;68:102253.
  • Mousavi SA, Chauvin A, Pascaud F, et al. GLUTAMATE RECEPTOR-LIKE genes mediate leaf-to-leaf wound signaling. Nature. 2013;500:422–426.
  • Nguyen CT, Kurenda A, Stolz S, et al. Identification of cell populations necessary for leaf-to-leaf electrical signaling in a wounded plant. Proc Natl Acad Sci U S A. 2018;115:10178–10183.
  • Alfieri A, Doccula FG, Pederzoli R, et al. The structural bases for agonist diversity in an Arabidopsis thaliana glutamate receptor-like channel. Proc Natl Acad Sci U S A. 2020;117:752–760.
  • Gangwar SP, Green MN, Michard E, et al. Structure of the Arabidopsis glutamate receptor-like channel GLR3.2 ligand-binding domain. Structure. 2021;29:161–169.
  • Green MN, Gangwar SP, Michard E, et al. Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4. Mol Cell. 2021;81:3216–3226.
  • Weiland M, Mancuso S, Baluska F. Signalling via glutamate and GLRs in Arabidopsis thaliana. Funct Plant Biol. 2015;43:1–25.
  • Wudick MM, Michard E, Oliveira Nunes C, et al. Comparing plant and animal glutamate receptors: common traits but different Fates? J Exp Bot. 2018;19. DOI:10.1093/jxb/ery153.
  • Grenzi M, Bonza MC, Alfieri A, et al. Structural insights into long-distance signal transduction pathways mediated by plant glutamate receptor-like channels. New Phytol. 2021;229:1261–1267.
  • Wu Q, Stolz S, Kumari A, et al. The carboxy-terminal tail of GLR3.3 is essential for wound-response electrical signaling. New Phytol. 2022;236:2189–2201.
  • Mousavi SA, Nguyen CT, Farmer EE, et al. Measuring surface potential changes on leaves. Nat Protoc. 2014;9:1997–2004.
  • Kurenda A, Farmer EE. Rapid extraction of living primary veins from the leaves of Arabidopsis thaliana. Protoc Exch. 2018. DOI:10.1038/protex.2018.119
  • Turgeon R, Wolf S. Phloem transport: cellular pathways and molecular trafficking. Annu Rev Plant Biol. 2009;60:207–221.
  • Cayla T, Batailler B, Le Hir R, et al. Live imaging of companion cells and sieve elements in Arabidopsis leaves. PLoS One. 2015;10:e0118122.
  • Jeffrey RA, Ch’ng TH, O’Dell TJ, et al. Activity-dependent anchoring of importin alpha at the synapse involves regulated binding to the cytoplasmic tail of the NR1-1a subunit of the NMDA receptor. J Neurosci. 2009;16:15613–15620.
  • Zhou L, Duan J. The C-terminus of NMDAR GluN1-1a Subunit translocates to nucleus and regulates synaptic function. Front Cell Neurosci. 2018;12:334.
  • Ch’ng TH, Martin KC. Synapse-to-nucleus signaling. Curr Opin Neurobiol. 2011;21:345–352.
  • Kumari A, Chételat A, Nguyen CT, et al. Arabidopsis H+-ATPase AHA1 controls slow wave potential duration and wound-response jasmonate pathway activation. Proc Natl Acad Sci U S A. 2019;116:20226–20231.
  • Pedersen PL. Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease. J Bioenerg Biomembr. 2007;39:349–355.
  • Speth C, Jaspert N, Marcon C, et al. Regulation of the plant plasma membrane H+-ATPase by its C-terminal domain: what do we know for sure? Eur J Cell Biol. 2010;89:145–151.
  • Palmgren MG, Larsson C, Sommarin M. Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment. J Biol Chem. 1990;265:13423–13426.
  • Zhao P, Zhao C, Chen D, et al. Structure and activation mechanism of the hexameric plasma membrane H+-ATPase. Nat Commun. 2021;12:6439.
  • Falhof J, Pedersen JT, Fuglsang AT, et al. Plasma membrane H+-ATPase regulation in the center of plant physiology. Mol Plant. 2016;9:323–337.
  • Fuglsang AT, Palmgren M. Proton and calcium pumping P-type ATPases and their regulation of plant responses to the environment. Plant Physiol. 2021;187:1856–1875.
  • Kosugi S, Hasebe M, Tomita M, et al. Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc Natl Acad Sci U S A. 2009;106:10171–10176.