An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

Hui, Norman; Nakamura, Nobuhiro; Sonnichsen, B.; Shima, David T.; Nilsson, Tommy; Warren, Graham

doi:10.1091/mbc.8.9.1777

Cited by 92 publications

(129 citation statements)

References 60 publications

(57 reference statements)

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“…5B). Depletion of syntaxin 5, which exists as two isoforms in vivo (39), gave a complete block in transport of VSV-G from the ER to the Golgi apparatus (Fig. 5, B and C).…”

Section: Resultsmentioning

confidence: 95%

Coordination of Golgin Tethering and SNARE Assembly

Diao

Frost

Morohashi

et al. 2008

Journal of Biological Chemistry

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During membrane traffic, transport carriers are first tethered to the target membrane prior to undergoing fusion. Mechanisms exist to connect tethering with fusion, but in most cases, the details remain poorly understood. GM130 is a member of the golgin family of coiled-coil proteins that is involved in membrane tethering at the endoplasmic reticulum (ER) to Golgi intermediate compartment and cis-Golgi. Here, we demonstrate that GM130 interacts with syntaxin 5, a t-SNARE also localized to the early secretory pathway. Binding to syntaxin 5 is specific, direct, and mediated by the membrane-proximal region of GM130. Interestingly, interaction with syntaxin 5 is inhibited by the binding of the vesicle docking protein p115 to a distal binding site in GM130. The interaction between GM130 and the small GTPase Rab1 is also inhibited by p115 binding. Our findings suggest a mechanism for coupling membrane tethering and fusion at the ER to Golgi intermediate compartment and cis-Golgi, with GM130 playing a central role in linking these processes. Consistent with this hypothesis, we find that depletion of GM130 by RNA interference slows the rate of ER to Golgi trafficking in vivo. The interactions of GM130 with syntaxin 5 and Rab1 are also regulated by mitotic phosphorylation, which is likely to contribute to the inhibition of ER to Golgi trafficking that occurs when mammalian cells enter mitosis.

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“…5B). Depletion of syntaxin 5, which exists as two isoforms in vivo (39), gave a complete block in transport of VSV-G from the ER to the Golgi apparatus (Fig. 5, B and C).…”

Section: Resultsmentioning

confidence: 95%

Coordination of Golgin Tethering and SNARE Assembly

Diao

Frost

Morohashi

et al. 2008

Journal of Biological Chemistry

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“…Fab antibodies directed at GOS 28 protein partially inhibit cell-free transport and accumulate tethered, uncoated COPI transport vesicles that fail to fuse (25). GOS 28 participates in a Golgi-restricted (28) SNARE complex with the short, Golgi-restricted spliced (29) form of Syntaxin 5 (30), suggesting the possibility that GOS 28 and the ''short'' form of the t-SNARE Syntaxin 5 comprise a SNARE complex (presumably with two other unidentified SNARE proteins) (5, 31) that promotes membrane fusion within the Golgi stack.…”

Section: Resultsmentioning

confidence: 99%

Anterograde flow of cargo across the Golgi stack potentially mediated via bidirectional “percolating” COPI vesicles

Orci

Ravazzola

Volchuk

et al. 2000

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

103

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How do secretory proteins and other cargo targeted to post-Golgi locations traverse the Golgi stack? We report immunoelectron microscopy experiments establishing that a Golgi-restricted SNARE, GOS 28, is present in the same population of COPI vesicles as anterograde cargo marked by vesicular stomatitis virus glycoprotein, but is excluded from the COPI vesicles containing retrograde-targeted cargo (marked by KDEL receptor). We also report that GOS 28 and its partnering t-SNARE heavy chain, syntaxin 5, reside together in every cisterna of the stack. Taken together, these data raise the possibility that the anterograde cargo-laden COPI vesicles, retained locally by means of tethers, are inherently capable of fusing with neighboring cisternae on either side. If so, quanta of exported proteins would transit the stack in GOS 28 -COPI vesicles via a bidirectional random walk, entering at the cis face and leaving at the trans face and percolating up and down the stack in between. Percolating vesicles carrying both post-Golgi cargo and Golgi residents up and down the stack would reconcile disparate observations on Golgi transport in cells and in cell-free systems.

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“…Western blotting was performed as described in Hui et al (1997). The rabbit anti-GM130 antiserum and affinity-purified MLO7, and the rabbit anti-p115 antiserum NN7 were detected with the use of anti-rabbit IgG coupled to horseradish peroxidase.…”

Section: Western Blottingmentioning

confidence: 99%

Biogenesis of Golgi Stacks in Imaginal Discs ofDrosophila melanogaster

Kondylis

Goulding

Dunne

et al. 2001

MBoC

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We provide a detailed description of Golgi stack biogenesis that takes place in vivo during one of the morphogenetic events in the lifespan of Drosophila melanogaster. In early third-instar larvae, small clusters consisting mostly of vesicles and tubules were present in epithelial imaginal disk cells. As larvae progressed through mid-and late-third instar, these larval clusters became larger but also increasingly formed cisternae, some of which were stacked. In white pupae, the typical Golgi stack was observed. We show that larval clusters are Golgi stack precursors by 1) localizing various Golgi-specific markers to the larval clusters by electron and immunofluorescence confocal microscopy, 2) driving this conversion in wild-type larvae incubated at 37°C for 2 h, and 3) showing that this conversion does not take place in an NSF1 mutant (comt 17). The biological significance of this conversion became clear when we found that the steroid hormone 20-hydroxyecdysone (ecdysone) is critically involved in this conversion. In its absence, Golgi stack biogenesis did not occur and the larval clusters remained unaltered. We showed that dGM130 and sec23p expression increases approximately three-and fivefold, respectively, when discs are exposed to ecdysone in vivo and in vitro. Taken together, these results suggest that we have developed an in vivo system to study the ecdysone-triggered Golgi stack biogenesis.

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An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

Cited by 92 publications

References 60 publications

Coordination of Golgin Tethering and SNARE Assembly

Coordination of Golgin Tethering and SNARE Assembly

Anterograde flow of cargo across the Golgi stack potentially mediated via bidirectional “percolating” COPI vesicles

Biogenesis of Golgi Stacks in Imaginal Discs ofDrosophila melanogaster

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