The measurement of exocytosis in plant cells

Battey, Nicholas H.; Carroll, Andrew; Kesteren, Pim Van; Taylor, Alison R.; Brownlee, Colin

doi:10.1093/jxb/47.6.717

Cited by 17 publications

(14 citation statements)

References 66 publications

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“…Hence an increase in membrane area would occur when the rate of exocytosis increases while membrane recycling remains constant [128]. The theoretical and technical aspects of the method have been reviewed in detail elsewhere [63,64,125,43,11 J.…”

Section: Measurement Of Whole Cell Membrane Capacitance: the Sum Of Ementioning

confidence: 99%

“…lular Ca2+ (e,g, [7]), GTP-binding proteins (e.g, [85]), cAMP (e.g, [102]) and CI~ [98] have been studied in animal cells. The same technique has also been introduced successfully into the repertoire of the plant electrophysiologist (reviewed in [11,51]). A wide range of indirect evidence implicated Ca2+ in the control of exocytosis in plants [107,12] so the effect of intracellular Ca2+ on exocytosis was addressed when the first electrophysiological studies of changes in membrane capacitance were made with aleurone pro-117 toplasts [126].…”

Section: Measurement Of Whole Cell Membrane Capacitance: the Sum Of Ementioning

confidence: 99%

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Exocytosis in plants

Thiel

Battey

1998

Protein Trafficking in Plant Cells

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Exocytosis is the final event in the secretory pathway and requires the fusion of the secretory vesicle membrane with the plasma membrane. It results in the release to the outside of vesicle cargo from the cell interior and also the delivery of vesicle membrane and proteins to the plasma membrane. An electrophysiological assay that measures changes in membrane capacitance has recently been used to monitor exocytosis in plants. This complements information derived from earlier light and electron microscope studies, and allows both transient and irreversible fusion of single exocytotic vesicles to be followed with high resolution in protoplasts. lt also provides a tool to investigate bulk exocytotic activity in single protoplasts under the infiuence of cytoplasmic modulators. This research highlights the role of intracellular Ca 2 +, GTP and pressure in the control of exocytosis in plants.In parallel to these functional studies, plant proteins with the potential to regulate exocytosis are being identified by molecular analysis. In this review we describe these electrophysiological and molecular advances, and emphasise the need for parallel biochemical work to provide a complete picture of the mechanisms controlling vesicle fusion at the plasma membrane of plant cells.

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Section: Measurement Of Whole Cell Membrane Capacitance: the Sum Of Ementioning

confidence: 99%

Section: Measurement Of Whole Cell Membrane Capacitance: the Sum Of Ementioning

confidence: 99%

Exocytosis in plants

Thiel

Battey

1998

Protein Trafficking in Plant Cells

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“…These processes sustain membrane protein turnover and thereby contribute to cellular homeostasis, differentiation, and growth. In plants, as in mammalian tissues, exocytotic and endocytotic events have been identified with stepwise changes in capacitance that accompany the increase or decrease of membrane surface area during vesicle membrane fusion and removal, respectively (Battey et al, 1996;Thiel and Battey, 1998). Factors affecting vesicle traffic in several instances have been shown to include cytosol-free Ca 2 ϩ concentration ([Ca 2 ϩ ] i ) and guanosine nucleotides (Homann and Tester, 1997;Carroll et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

The Abscisic Acid–Related SNARE Homolog NtSyr1 Contributes to Secretion and Growth

et al. 2002

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Syntaxins and other SNARE proteins are crucial for intracellular vesicle trafficking, fusion, and secretion. Previously, we isolated the syntaxin-related protein NtSyr1 (NtSyp121) from tobacco in a screen for abscisic acid-related signaling elements, demonstrating its role in determining the abscisic acid sensitivity of K ؉ and Cl ؊ channels in stomatal guard cells. NtSyr1 is localized to the plasma membrane and is expressed normally throughout the plant, especially in root tissues, suggesting that it might contribute to cellular homeostasis as well as to signaling. To explore its functions in vivo further, we examined stably transformed lines of tobacco that expressed various constructs of NtSyr1 , including the full-length protein and a truncated fragment, Sp2, corresponding to the cytosolic domain shown previously to be active in suppressing ion channel response to abscisic acid. Constitutively overexpressing NtSyr1 yielded uniformly high levels of protein ( Ͼ 10 times the wild-type levels) and was associated with a significant enhancement of root growth in seedlings but not with any obvious phenotype in mature, well-watered plants. Similar transformations with constructs encoding the Sp2 fragment of NtSyr1 showed altered leaf morphology but gave only low levels of Sp2 fragment, suggesting a strong selective pressure against plants expressing this protein. High expression of the Sp2 fragment was achieved in stable transformants under the control of a dexamethasone-inducible promoter. Sp2 expression was correlated positively with altered cellular and tissue morphology in leaves and roots and with a cessation of growth in seedlings. Overexpression of the full-length NtSyr1 protein rescued the wild-type phenotype, even in plants expressing high levels of the Sp2 fragment, supporting the idea that the Sp2 fragment interfered specifically with NtSyr1 function by competing with NtSyr1 for its binding partners. To explore NtSyr1 function in secretion, we used a green fluorescent protein (GFP)-based section assay. When a secreted GFP marker was coexpressed with Sp2 in tobacco leaves, GFP fluorescence was retained in cytosolic reticulate and punctate structures. In contrast, in plants coexpressing secreted GFP and NtSyr1 or secreted GFP alone, no GFP fluorescence accumulated within the cells. A new yellow fluorescent protein-based secretion marker was used to show that the punctate structures labeled in the presence of Sp2 colocalized with a Golgi marker. These structures were not labeled in the presence of a dominant Rab1 mutant that inhibited transport from the endoplasmic reticulum to the Golgi. We propose that NtSyr1 functions as an element in SNARE-mediated vesicle trafficking to the plasma membrane and is required for cellular growth and homeostasis. INTRODUCTIONMembrane trafficking to and from the plasma membrane in all eukaryotic cells is mediated by exocytotic and endocytotic fusion of vesicles from endosomal compartments. These processes sustain membrane protein turnover and 1 These authors contributed equal...

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“…As all cells studied in the current work had started to vacuolate (see Results), they were likely to be in the process of exocytosis. By using the patch-clamp technique, we have monitored changes in plasma membrane area, resulting from endo-and exocytotic events, by measuring the membrane capacitance (C m ) (14,15 …”

mentioning

confidence: 99%

Ca ²⁺ -independent and Ca ²⁺ /GTP-binding protein-controlled exocytosis in a plant cell

Homann

Tester

1997

Proc. Natl. Acad. Sci. U.S.A.

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The measurement of exocytosis in plant cells

Cited by 17 publications

References 66 publications

Exocytosis in plants

Exocytosis in plants

The Abscisic Acid–Related SNARE Homolog NtSyr1 Contributes to Secretion and Growth

Ca ²⁺ -independent and Ca ²⁺ /GTP-binding protein-controlled exocytosis in a plant cell

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The measurement of exocytosis in plant cells

Cited by 17 publications

References 66 publications

Exocytosis in plants

Exocytosis in plants

The Abscisic Acid–Related SNARE Homolog NtSyr1 Contributes to Secretion and Growth

Ca 2+ -independent and Ca 2+ /GTP-binding protein-controlled exocytosis in a plant cell

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Ca ²⁺ -independent and Ca ²⁺ /GTP-binding protein-controlled exocytosis in a plant cell