Ca2+ Conduction by an Amino Acid-Gated Ion Channel Related to Glutamate Receptors

Vincill, Eric D.; Bieck, Anthony M.; Spalding, Edgar P.

doi:10.1104/pp.112.197509

Cited by 138 publications

(158 citation statements)

References 49 publications

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“…Two separate approaches using Förster Resonance Energy Transfer (FRET) identified homomeric interactions for GLR1.1 and GLR3.4. GLR3.4 has been shown to function as a Ca 2+ -conducting channel when expressed in HEK293 cells in a previous work, 27 corroborating the finding in this study. In contrast to the results published from the same group, however, we did not observe consistent interaction between GLR3.2 and GLR3.4.…”

Section: Discussionsupporting

confidence: 82%

“…17 Understanding the function of plant GLRs has previously been hampered by gene redundancy and toxicity although genetic, pharmacological, and electrophysiological approaches suggested diverse physiological roles such as carbon/nitrogen balance regulation, 18,19 stomatal opening, 20 pollen tube growth, 21 plant-pathogen interaction, [22][23][24] responses to wound, 25,26 and lateral root formation. 12 Recently, 2 of the Arabidopsis GLRs, AtGLR3.4 and 1.4, were shown to function as amino acid gated channels when expressed in heterologous systems, 13,27 further confirming the functional commonality of plant and mammalian glutamate receptors.…”

Section: Introductionmentioning

confidence: 69%

“…Homomeric interactions were consistently observed for GLR1.1NubG/GLR1.1Cub and GLR2.1NubG/GLR2.1Cub (Table S1). Interestingly, homomeric interaction for GLR1.4NubG/GLR1.4Cub and GLR3.4NubG/GLR3.4Cub, the subunits capable of acting as homomeric channels in heterologous expression systems, 13,27 were not among the strongest interactions observed ( Fig. 1; Table S1).…”

Section: Split Ubiquitin Systemmentioning

confidence: 99%

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Inter-subunit interactions between Glutamate-Like Receptors inArabidopsis

Price

Kong

Okumoto

2013

Plant Signaling & Behavior

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Section: Discussionsupporting

confidence: 82%

Section: Introductionmentioning

confidence: 69%

Section: Split Ubiquitin Systemmentioning

confidence: 99%

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Inter-subunit interactions between Glutamate-Like Receptors inArabidopsis

Price

Kong

Okumoto

2013

Plant Signaling & Behavior

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“…HEK Cell Culture, ABCB19 Expression, and Electrophysiology HEK 293T cells were cultured in dishes on coverslips and transfected as described (Vincill et al, 2012). ABCB19 cDNA was amplified from cDNA template using primers 59-ACAAGTCGACATGTCGGAAACTAACACAAC-39 and 59-ACTGCCCGGGTCAAATCCTATGTGTTTG-39, then inserted into the SalI and XmaI sites (underlined sequences) of the pIRES-Enhanced Green Fluorescent Protein (EGFP) bicistronic vector used by Vincill et al (2012) such that a single mRNA would separately code ABCB19 and EGFP.…”

Section: Methodsmentioning

confidence: 99%

“…ABCB19 cDNA was amplified from cDNA template using primers 59-ACAAGTCGACATGTCGGAAACTAACACAAC-39 and 59-ACTGCCCGGGTCAAATCCTATGTGTTTG-39, then inserted into the SalI and XmaI sites (underlined sequences) of the pIRES-Enhanced Green Fluorescent Protein (EGFP) bicistronic vector used by Vincill et al (2012) such that a single mRNA would separately code ABCB19 and EGFP. To produce the G-to-A mutation at +3,517 that generates the ABCB19 D1173N allele, one-step reverse transcription-PCR was performed on mRNA isolated from abcb19-6 mutant seedlings (see below) to obtain a portion of the ABCB19 gene (+3,101 from ATG to +3,759) using primers 59-CTCAGAATTCGAGCTGGACATAGCCAA-39 and 59-ACTGCCCGGGTCAAATCCTATGTGTTTG-39.…”

Section: Methodsmentioning

confidence: 99%

Block of ATP-Binding Cassette B19 Ion Channel Activity by 5-Nitro-2-(3-Phenylpropylamino)-Benzoic Acid Impairs Polar Auxin Transport and Root Gravitropism

et al. 2014

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Polar transport of the hormone auxin through tissues and organs depends on membrane proteins, including some B-subgroup members of the ATP-binding cassette (ABC) transporter family. The messenger RNA level of at least one B-subgroup ABCB gene in Arabidopsis (Arabidopsis thaliana), ABCB19, increases upon treatment with the anion channel blocker 5-nitro-2-(3-phenylpropylamino)-benzoic acid (NPPB), possibly to compensate for an inhibitory effect of the drug on ABCB19 activity. Consistent with this hypothesis, NPPB blocked ion channel activity associated with ABCB19 expressed in human embryonic kidney cells as measured by patch-clamp electrophysiology. NPPB inhibited polar auxin transport through Arabidopsis seedling roots similarly to abcb19 mutations. NPPB also inhibited shootward auxin transport, which depends on the related ABCB4 protein. NPPB substantially decreased ABCB4 and ABCB19 protein levels when cycloheximide concomitantly inhibited new protein synthesis, indicating that blockage by NPPB enhances the degradation of ABCB transporters. Impairing the principal auxin transport streams in roots with NPPB caused aberrant patterns of auxin signaling reporters in root apices. Formation of the auxin-signaling gradient across the tips of gravity-stimulated roots, and its developmental consequence (gravitropism), were inhibited by micromolar concentrations of NPPB that did not affect growth rate. These results identify ion channel activity of ABCB19 that is blocked by NPPB, a compound that can now be considered an inhibitor of polar auxin transport with a defined molecular target.

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Electrophysiological study of Arabidopsis ABCB4 and PIN2 auxin transporters: Evidence of auxin activation and interaction enhancing auxin selectivity

Deslauriers

Spalding

2021

Plant Direct

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Polar auxin transport through plant tissue strictly requires polarly localized PIN proteins and uniformly distributed ABCB proteins. A functional synergy between the two types of membrane protein where their localizations overlap may create the degree of asymmetric auxin efflux required to produce polar auxin transport. We investigated this possibility by expressing ABCB4 and PIN2 in human embryonic kidney cells and measuring whole‐cell ionic currents with the patch‐clamp technique and CsCl‐based electrolytes. ABCB4 activity was 1.81‐fold more selective for Cl− over Cs+ and for PIN2 the value was 2.95. We imposed auxin gradients and determined that ABCB4 and PIN2 were 12‐fold more permeable to the auxin anion (IAA−) than Cl−. This measure of the intrinsic selectivity of the transport pathway was 21‐fold when ABCB4 and PIN2 were co‐expressed. If this increase occurs in plants, it could explain why asymmetric PIN localization is not sufficient to create polar auxin flow. Some form of co‐action or synergy between ABCB4 and PIN2 that increases IAA− selectivity at the cell face where both occur may be important. We also found that auxin stimulated ABCB4 activity, which may contribute to a self‐reinforcement of auxin transport known as canalization.

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Ca2+ Conduction by an Amino Acid-Gated Ion Channel Related to Glutamate Receptors

Cited by 138 publications

References 49 publications

Inter-subunit interactions between Glutamate-Like Receptors inArabidopsis

Inter-subunit interactions between Glutamate-Like Receptors inArabidopsis

Block of ATP-Binding Cassette B19 Ion Channel Activity by 5-Nitro-2-(3-Phenylpropylamino)-Benzoic Acid Impairs Polar Auxin Transport and Root Gravitropism

Electrophysiological study of Arabidopsis ABCB4 and PIN2 auxin transporters: Evidence of auxin activation and interaction enhancing auxin selectivity

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