SNARE complexes of different composition jointly mediate membrane fusion in<i>Arabidopsis</i>cytokinesis

Kasmi, Farid El; Krause, Cornélia; Hiller, Ulrike; Stierhof, York‐Dieter; Mayer, Ulríke; Conner, Lindsey; Kong, Lingtian; Reichardt, Ilka; Sanderfoot, Anton A.; Jürgens, Gerd

doi:10.1091/mbc.e13-02-0074

Cited by 112 publications

(142 citation statements)

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“…A key event in cell plate formation is vesicle fusion mediated by SNARE complexes (El Kasmi et al, 2013), with the complex formed by the Q-SNARE KNOLLE and the R-SNAREs Vesicle-Associated Membrane Protein721 (VAMP721) or VAMP722 playing a preponderant role (Lauber et al, 1997;Zhang et al, 2011). Additional proteins in this complex include the SEC1/Munc18 protein KEULLE, SNAP33, and NPSN11 (Assaad et al, 2001;Heese et al, 2001;Zheng et al, 2002).…”

Section: Tgn and The Cell Plate: A Timely Connectionmentioning

confidence: 99%

The Plant Trans-Golgi Network: Not Just a Matter of Distinction

2017

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Section: Tgn and The Cell Plate: A Timely Connectionmentioning

confidence: 99%

The Plant Trans-Golgi Network: Not Just a Matter of Distinction

2017

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“…Since diffusion-based growth with ideal vesicle fusion kinetics is enough to support cell growth, we sought to estimate the true kinetics of vesicle membrane fusion during exocytosis. Docking and fusion of exocytic vesicles is a multistep process mediated by protein complexes such as Exocyst (Kulich et al, 2010;Bloch et al, 2016) and the SNARE complex (Lipka et al, 2007;El Kasmi et al, 2013), which we simplify by assuming that VAMP72 vesicles interact with one type of receptor on the plasma membrane at the cell tip. We also assume that this type of receptor has one reaction rate and facilitates the integration of vesicles into the plasma membrane.…”

Section: Vesicle Concentrations Yield An Estimate Of Vesicle Fusion Kmentioning

confidence: 99%

F-Actin Mediated Focusing of Vesicles at the Cell Tip Is Essential for Polarized Growth

et al. 2017

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(L.V.).F-actin has been shown to be essential for tip growth in an array of plant models, including Physcomitrella patens. One hypothesis is that diffusion can transport secretory vesicles, while actin plays a regulatory role during secretion. Alternatively, it is possible that actin-based transport is necessary to overcome vesicle transport limitations to sustain secretion. Therefore, a quantitative analysis of diffusion, secretion kinetics, and cell geometry is necessary to clarify the role of actin in polarized growth. Using fluorescence recovery after photobleaching analysis, we first show that secretory vesicles move toward and accumulate at the tip in an actin-dependent manner. We then depolymerized F-actin to decouple vesicle diffusion from actin-mediated transport and measured the diffusion coefficient and concentration of vesicles. Using these values, we constructed a theoretical diffusion-based model for growth, demonstrating that with fast-enough vesicle fusion kinetics, diffusion could support normal cell growth rates. We further refined our model to explore how experimentally extrapolated vesicle fusion kinetics and the size of the secretion zone limit diffusion-based growth. This model predicts that diffusion-mediated growth is dependent on the size of the region of exocytosis at the tip and that diffusion-based growth would be significantly slower than normal cell growth. To further explore the size of the secretion zone, we used a cell wall degradation enzyme cocktail and determined that the secretion zone is smaller than 6 mm in diameter at the tip. Taken together, our results highlight the requirement for active transport in polarized growth and provide important insight into vesicle secretion during tip growth.

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“…The plasma membrane (PM) SNARE Syntaxin of Plants121 (SYP121; Leyman et al, 1999), vesicle-and PM-localized Vesicle-Associated Membrane Protein721 (VAMP721; El Kasmi et al, 2013), and endoplasmic reticulum-localized SNARE VAMP723 (Uemura et al, 2004) were used here to assess the vector potential for (co)localization studies. Figure 3 and Supplemental Figure S1 demonstrate the use of pFRETgc 2in1 vectors to determine and distinguish the subcellular localization of the aforementioned proteins while using different transformation procedures and hosts.…”

Section: Dual Expression From One T-dnamentioning

confidence: 99%

“…Despite heterologous overexpression, all gene products localize to their previously suggested, native subcellular compartments (Leyman et al, 1999;Uemura et al, 2004;El Kasmi et al, 2013). The vector set was primarily anticipated for transient studies in which the 35S promoter is still a powerful driver of expression despite its inherent silencing issues when used in stable transformants (Chalfun-Junior et al, 2003).…”

Section: Dual Expression From One T-dnamentioning

confidence: 99%

Binary 2in1 Vectors Improve in Planta (Co)localization and Dynamic Protein Interaction Studies

Hecker

Wallmeroth²,

Peter³

et al. 2015

Plant Physiol.

100

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Fluorescence-based protein-protein interaction techniques are vital tools for understanding in vivo cellular functions on a mechanistic level. However, only under the condition of highly efficient (co)transformation and accumulation can techniques such as Förster resonance energy transfer (FRET) realize their potential for providing highly accurate and quantitative interaction data. FRET as a fluorescence-based method unifies several advantages, such as measuring in an in vivo environment, real-time context, and the ability to include transient interactions as well as detecting the mere proximity of proteins. Here, we introduce a novel vector set that incorporates the benefit of the recombination-based 2in1 cloning system with the latest state-of-the-art fluorescent proteins for optimal coaccumulation and FRET output studies. We demonstrate its utility across a range of methods. Merging the 2in1 cloning system with new-generation FRET fluorophore pairs allows for enhanced detection, speeds up the preparation of clones, and enables colocalization studies and the identification of meaningful protein-protein interactions in vivo.Two technological advances allowed the field of modern cell biology to emerge: the development of high-resolution microscopes and the groundbreaking work in the development of fluorescent proteins (FPs) that were originally isolated from jellyfish (for review, see Day and Davidson, 2009;Zimmer, 2009). Genetically encoded FPs can be fused directly to proteins of choice, offering insights into their functional properties by allowing researchers to monitor subcellular localization, chemical environment, interaction, movement, and/or turnover rate.Research on the FPs themselves has exploded in the past two decades, and a range of technological improvements to and variations of the FPs were generated. These improvements include novel spectral properties from all areas of the color palette and from a diverse range of organisms. They also extend to a multitude of parameters, such as brightness, folding efficiency, chromophore oxidation rate, quantum yield, pH, and photostability (Day and Davidson, 2009). Taken together, these optimizations further the possibilities of available methods or prompt the development of new techniques.In 1946, the German scientist Theodor Förster laid the theoretical foundation for resonance energy transfer, now known as Förster resonance energy transfer (FRET;Forster, 1946). According to this theory, a donor chromophore in an excited state can transfer the excitation energy to a nearby acceptor chromophore via dipole-dipole coupling without the emission of a photon (for review, see Clegg, 2009;Ishikawa-Ankerhold et al., 2012). FRET depends on the spectral overlap between the emission spectrum of the donor and the absorbance spectrum of the acceptor chromophores. It also depends on the fluorescence quantum yield and the excited state lifetime of the donor in the absence of an acceptor as well as the relative orientation of the two chromophores. Most importantly, FRET ef...

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SNARE complexes of different composition jointly mediate membrane fusion inArabidopsiscytokinesis

Cited by 112 publications

References 40 publications

The Plant Trans-Golgi Network: Not Just a Matter of Distinction

The Plant Trans-Golgi Network: Not Just a Matter of Distinction

F-Actin Mediated Focusing of Vesicles at the Cell Tip Is Essential for Polarized Growth

Binary 2in1 Vectors Improve in Planta (Co)localization and Dynamic Protein Interaction Studies

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