Characterization of a cis-Golgi matrix protein, GM130.

Nakamura, Nobuhiro; Rabouille, Cathérine; Watson, Rose; Nilsson, Tommy; Hui, Norman; Slusarewicz, Paul; Kreis, Thomas E.; Warren, Graham

doi:10.1083/jcb.131.6.1715

Cited by 758 publications

(742 citation statements)

References 61 publications

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“…GM130 is one of the fast-moving proteins during BFA recovery (Jiang et al, 2006). As reported previously (Nakamura et al, 1995;Seemann et al, 2000;Ward et al, 2001), GM130 was distributed in punctate structures in BFA-treated cells (Supplemental Figure S3, second row). Although previous studies showed that combined treatment of normal rat kidney or HeLa cells with BFA followed by BFA plus H89 causes ER localization of GM130 (Puri and Linstedt, 2003;Jiang et al, 2006), such redistribution was not observed in COS-7 cells when 50 M H89 in addition to 10 M BFA was used (data not shown).…”

supporting

confidence: 80%

“…As shown in Supplemental Figure S2, in Noc-treated cells, Bap31 did not accumulate at ER exit sites defined by Sec31A (third row), but remained within the ER where SERCA2 was present (second row) upon H89 treatment. H89 treatment did not affect the exit site localization of ␤-COP (fourth row) or a Golgi marker, GM130 (Nakamura et al, 1995) (bottom row), in Noc-treated cells. These results sup- port the idea that the transport of Bap31 occurs not through the conventional transport pathway.…”

Section: Bap31 Accumulates At the Juxtanuclear Region By H89 Treatmentmentioning

confidence: 99%

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Bap31 Is an Itinerant Protein That Moves between the Peripheral Endoplasmic Reticulum (ER) and a Juxtanuclear Compartment Related to ER-associated Degradation

Wakana

Takai

Nakajima

et al. 2008

MBoC

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Certain endoplasmic reticulum (ER)-associated degradation (ERAD) substrates with transmembrane domains are segregated from other ER proteins and sorted into a juxtanuclear subcompartment, known as the ER quality control compartment. Bap31 is an ER protein with three transmembrane domains, and it is assumed to be a cargo receptor for ER export of some transmembrane proteins, especially those prone to ERAD. Here, we show that Bap31 is a component of the ER quality control compartment and that it moves between the peripheral ER and a juxtanuclear ER or ER-related compartment distinct from the conventional ER-Golgi intermediate compartment. The third and second transmembrane domains of Bap31 are principally responsible for the movement to and recycling from the juxtanuclear region, respectively. This cycling was blocked by depolymerization of microtubules and disruption of dynein-dynactin function. Overexpression of Sar1p and Arf1 mutants affected Bap31 cycling, suggesting that this cycling pathway is related to the conventional vesicular transport pathways. INTRODUCTIONThe endoplasmic reticulum (ER) exhibits a reticular tubular network that extends from the nucleus to the cell periphery along microtubule tracks. It performs a variety of functions, including the synthesis, posttranslational modifications, quality control, and export of secretory and membrane proteins; the synthesis of lipids; stress response; Ca 2ϩ storage; and apoptosis. Most, if not all, of these functions are managed by subdomains, such as the rough and smooth ER and transitional ER sites. Each subdomain contains a unique set of proteins that are responsible for its function and organization. ER subdomains are relatively stable, but they can be transformed into alternative structures in response to cellular conditions (for review, see Voeltz et al., 2002;Levine and Rabouille, 2005;Borgese et al., 2006;Vedrenne and Hauri, 2006).Several studies showed the presence of a specialized ER subdomain that is related to ER-associated degradation (ERAD). ERAD is part of a quality control system that ensures the delivery of only correctly folded or assembled secretory and membrane proteins to their final destinations. Newly synthesized proteins that fail to fold or assemble correctly are retained in the ER, retrotranslocated to the cytosol, and degraded by the ubiquitin-proteasome system (for review, see Ellgaard and Helenius, 2003;Meusser et al., 2005;Rö misch, 2005). Studies using mammalian cells demonstrated that transmembrane ERAD substrates are segregated into "ER quality control compartments," which become discernible at the juxtanuclear region upon inhibition of ERAD by proteasome inhibitors (Kamhi-Nesher et al., 2001;Spiliotis et al., 2002). In Saccharomyces cerevisiae, ectopically expressed cystic fibrosis transmembrane conductance regulator (CFTR) is segregated from other ER proteins and accumulates in ER-associated compartments (Kiser et al., 2001;Zhang et al., 2001;Huyer et al., 2004). Degradation of CFTR in yeast is independent of ER-to-Golgi tr...

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supporting

confidence: 80%

Section: Bap31 Accumulates At the Juxtanuclear Region By H89 Treatmentmentioning

confidence: 99%

Bap31 Is an Itinerant Protein That Moves between the Peripheral Endoplasmic Reticulum (ER) and a Juxtanuclear Compartment Related to ER-associated Degradation

Wakana

Takai

Nakajima

et al. 2008

MBoC

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“…[91][92][93] The very C-terminus of GM130 may bind to and stimulate the catalytic activity of HtrA1, a serine protease that inhibits TGF-b signaling. 94 EspG proteins produced by enteric pathogens may interact with GM130 and disrupt protein secretion of the host cells.…”

Section: Gcks In Immune Regulationmentioning

confidence: 99%

Germinal center kinases in immune regulation

Yin

Shi

et al. 2012

Cell Mol Immunol

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“…The rabbit polyclonal MLO7 antibody (gift from M. Lowe, Manchester, United Kingdom) was raised against the first 73 amino acids of human GM130 (Nakamura et al, 1995;Lowe et al, 1998), a Golgi peripheral membrane protein receptor for p115 (Nakamura et al, 1997, see below). The corresponding 73 amino acids in the predicted Drosophila homolog of GM130 (AJ276417, CG11061) are 40% identical and 51% similar to human and rat GM130 with a very strong conservation in the first 25 (up to 64% identity and 84% similarity).…”

Section: Drosophila Golgi Markers and Antibodiesmentioning

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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Characterization of a cis-Golgi matrix protein, GM130.

Cited by 758 publications

References 61 publications

Bap31 Is an Itinerant Protein That Moves between the Peripheral Endoplasmic Reticulum (ER) and a Juxtanuclear Compartment Related to ER-associated Degradation

Bap31 Is an Itinerant Protein That Moves between the Peripheral Endoplasmic Reticulum (ER) and a Juxtanuclear Compartment Related to ER-associated Degradation

Germinal center kinases in immune regulation

Biogenesis of Golgi Stacks in Imaginal Discs ofDrosophila melanogaster

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