Membrane Protein Transport between the Endoplasmic Reticulum and the Golgi in Tobacco Leaves Is Energy Dependent but Cytoskeleton Independent

Brandizzí, Federica; Snapp, Erik L.; Roberts, Alison G.; Lippincott‐Schwartz, Jennifer; Hawes, Chris

doi:10.1105/tpc.001586

Cited by 296 publications

(397 citation statements)

References 62 publications

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“…Collectively, these findings are consistent with the proposal that the intracellular transport of TMV occurs via the ER and that the adjacent actin cytoskeleton may exert control over ER-mediated transport via myosin bridges. The observation that transient ABD2:GFP expression interfered with myosin-mediated motility is in agreement with several other reports indicating that the expression of GFP fusions with actin-binding proteins can interfere with actin dynamics and organization, even though they are valuable tools for evaluating cytoskeletal functions (Kost et al, 1998;Mathur et al, 1999;Fu et al, 2001;Brandizzi et al, 2002;Ilgenfritz et al, 2003;Holweg et al, 2004;Ketelaar et al, 2004;Weerasinghe et al, 2005;Xu and Scheres, 2005;Holweg, 2007;Wang et al, 2008). The inhibition of myosin-based dynamics upon transient expression of ABD2:GFP in our N. benthamiana system is probably related to the ABD2:GFP expression level, which during the time of the experiment (1.5 and 2.5 dpa) was in excess of the level of ABD2:GFP in transgenic plants.…”

Section: Discussionsupporting

confidence: 78%

“…2C) and is highly dynamic. A dynamic ER network was also revealed by time-lapse analysis of wildtype plants in which the ER was labeled by transient expression of GFP:HDEL, RFP:HDEL, or TM17:GFP, an ER transmembrane peptide fused to GFP (Brandizzi et al, 2002; data not shown). Transient expression of RFP:HDEL in ABD2:GFP transgenic plants revealed that transgenic ABD2:GFP expression does not interfere with the structure and dynamic movements of the ER (Fig.…”

Section: Labeling Of Actin Filaments With Abd:gfpmentioning

confidence: 99%

“…The motility of Golgi stacks depends on specific class XI myosins (Avisar et al, 2008b;Peremyslov et al, 2008;Prokhnevsky et al, 2008;Sparkes et al, 2008), requires an intact and dynamic actin cytoskeleton (Nebenfü hr et al, 1999;Brandizzi et al, 2002), and appears to occur with the membranes of the ER (Runions et al, 2006). To investigate whether expression of ABD2:GFP affects actin-myosin-based Golgi motility, we monitored the motility of Golgi stacks upon transient expression of the red fluorescent, tdTomato-tagged, cis-Golgi marker GmMan1 (GmMan1: tdTomato;Nebenfü hr et al, 1999;Fig.…”

Section: Labeling Of Actin Filaments With Abd:gfpmentioning

confidence: 99%

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Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein

et al. 2009

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The tobacco mosaic virus (TMV) movement protein (MP) required for the cell-to-cell spread of viral RNA interacts with the endoplasmic reticulum (ER) as well as with the cytoskeleton during infection. Whereas associations of MP with ER and microtubules have been intensely investigated, research on the role of actin has been rather scarce. We demonstrate that Nicotiana benthamiana plants transgenic for the actin-binding domain 2 of Arabidopsis (Arabidopsis thaliana) fimbrin (AtFIM1) fused to green fluorescent protein (ABD2:GFP) exhibit a dynamic ABD2:GFP-labeled actin cytoskeleton and myosin-dependent Golgi trafficking. These plants also support the movement of TMV. In contrast, both myosin-dependent Golgi trafficking and TMV movement are dominantly inhibited when ABD2:GFP is expressed transiently. Inhibition is mediated through binding of ABD2:GFP to actin filaments, since TMV movement is restored upon disruption of the ABD2:GFP-labeled actin network with latrunculin B. Latrunculin B shows no significant effect on the spread of TMV infection in either wild-type plants or ABD2:GFP transgenic plants under our treatment conditions. We did not observe any binding of MP along the length of actin filaments.Collectively, these observations demonstrate that TMV movement does not require an intact actomyosin system. Nevertheless, actin-binding proteins appear to have the potential to exert control over TMV movement through the inhibition of myosinassociated protein trafficking along the ER membrane.The mechanism by which plant viruses move from cell to cell and systemically to cause systemic infection has been the subject of intense studies (for review, see

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Section: Discussionsupporting

confidence: 78%

Section: Labeling Of Actin Filaments With Abd:gfpmentioning

confidence: 99%

Section: Labeling Of Actin Filaments With Abd:gfpmentioning

confidence: 99%

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Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein

et al. 2009

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“…It probably works with the COPII machinery but a COPII independent pathway is also possible [49]. Surprisingly, the transfer from ER to Golgi is independent of actin or microtubules [50]. The long-standing contact between the reticulum and the Golgi is apparently sufficient to support the transfer.…”

Section: Reticulum and Golgi Exchangesmentioning

confidence: 99%

Glycerolipid transfer for the building of membranes in plant cells

Jouhet

Maréchal

Block

2007

Progress in Lipid Research

134

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“…Graphs were prepared with KaleidaGraph (Synergy Software, Reading, PA). The mobile fraction was calculated as follows (Ellenberg et al, 1997;Brandizzi et al, 2002) …”

mentioning

confidence: 99%

Dynamic Movement of the Calcium Sensor STIM1 and the Calcium Channel Orai1 in Activated T-Cells: Puncta and Distal Caps

Barr

Bernot

Srikanth

et al. 2008

MBoC

129

142

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The proteins STIM1 and Orai1 are the long sought components of the store-operated channels required in T-cell activation. However, little is known about the interaction of these proteins in T-cells after engagement of the T-cell receptor. We found that T-cell receptor engagement caused STIM1 and Orai1 to colocalize in puncta near the site of stimulation and accumulate in a dense structure on the opposite side of the T-cell. FRET measurements showed a close interaction between STIM1 and Orai1 both in the puncta and in the dense cap-like structure. The formation of cap-like structures did not entail rearrangement of the entire endoplasmic reticulum. Cap formation depended on TCR engagement and tyrosine phosphorylation, but not on channel activity or Ca 2؉ influx. These caps were very dynamic in T-cells activated by contact with superantigen pulsed B-cells and could move from the distal pole to an existing or a newly forming immunological synapse. One function of this cap may be to provide preassembled Ca 2؉ channel components to existing and newly forming immunological synapses. INTRODUCTIONT-cell activation in response to antigen induces and requires the elevation of intracellular Ca 2ϩ (Hogan et al., 2003;Quintana et al., 2005;Feske, 2007). T-cell receptor (TCR) engagement leads to activation of well-documented signal transduction pathways that cause a rapid release of Ca 2ϩ from the endoplasmic reticulum (ER; Samelson, 2002;Panyi et al., 2004;Gwack et al., 2007a). The depletion of Ca 2ϩ from this internal store then leads to the opening of ion channels in the plasma membrane (PM) allowing an influx of Ca 2ϩ from outside the cell. The store-operated channel responsible for Ca 2ϩ influx in T-cells is known as the Ca 2ϩ release-activated Ca 2ϩ (CRAC) channel, which has been studied by electrophysiological techniques for many years (Lewis, 2001;Prakriya and Lewis, 2003;Cahalan et al., 2007;Hewavitharana et al., 2007;Hogan and Rao, 2007;Putney, 2007a).Sustained elevation of cytosolic Ca 2ϩ is required for complete T-cell activation (Iezzi et al., 1998;Lewis, 2001;Hogan et al., 2003;Feske, 2007). High levels of intracellular Ca 2ϩ are necessary to maintain the interaction between a T-cell and antigen-presenting cell (APC) that leads to formation of the specialized contact surface known as the immunological synapse (IS). Increased Ca 2ϩ levels are also required for the activation of transcription factors. In particular, elevated Ca 2ϩ maintains prolonged nuclear accumulation of nuclear factor of activated T-cells (NFAT) by activating the phosphatase calcineurin that dephosphorylates NFAT, allowing it to translocate to the nucleus and activate genes such as IL2 (Hogan et al., 2003;Macian, 2005). Several hours of Ca 2ϩ influx are required to complete the T-cell activation program, which involves expression of a large number of activation-associated genes (Lewis, 2001;Macian et al., 2002;Hogan et al., 2003).Although sustained Ca 2ϩ influx in T-cells has been studied for decades, the proteins involved have only been ident...

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Membrane Protein Transport between the Endoplasmic Reticulum and the Golgi in Tobacco Leaves Is Energy Dependent but Cytoskeleton Independent

Cited by 296 publications

References 62 publications

Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein

Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein

Glycerolipid transfer for the building of membranes in plant cells

Dynamic Movement of the Calcium Sensor STIM1 and the Calcium Channel Orai1 in Activated T-Cells: Puncta and Distal Caps

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