The Gos28 SNARE Protein Mediates Intra-Golgi Transport of Rhodopsin and Is Required for Photoreceptor Survival

Rosenbaum, Erica E.; Vasiljevic, Eva; Cleland, Spencer C.; Flores, Carlos; Colley, Nansi Jo

doi:10.1074/jbc.m114.585166

Cited by 17 publications

(16 citation statements)

References 79 publications

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“…Membrane proteins synthesized on the ER membrane are transported to cis- Golgi cisternae by Rab1 (Satoh et al, 1997), Syx5, and possibly by Sec22 (Zhao et al, 2015). Probably after Gos28 dependent processes (Rosenbaum et al, 2014), basolateral membrane proteins are sorted by AP1 at trans- Golgi/TGN (Satoh et al, 2013) and the two apical membrane proteins are transported together to the recycling endosome (RE) by Rab6 (Iwanami et al, 2016). There is another round of sorting for the two apical pathways at the RE.…”

Section: Discussionmentioning

confidence: 99%

“…SNAREs seem to mediate membrane fusion in all the trafficking steps of the secretory pathway, except the fusion events in mitochondria and peroxisomes. Recent studies have identified two SNARE proteins, Sec22 and Gos28, which play essential roles in transporting Rh1 to the rhabdomeres (Rosenbaum et al, 2014; Zhao et al, 2015). An extensive Rh1 transport assay revealed that Gos28 is involved in intra-Golgi transport downstream of alpha-mannosidase-II in medial - Golgi (Rosenbaum et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…Recent studies have identified two SNARE proteins, Sec22 and Gos28, which play essential roles in transporting Rh1 to the rhabdomeres (Rosenbaum et al, 2014; Zhao et al, 2015). An extensive Rh1 transport assay revealed that Gos28 is involved in intra-Golgi transport downstream of alpha-mannosidase-II in medial - Golgi (Rosenbaum et al, 2014). It was also reported that Gos28 mutation affects the modification and transport of Rh1, but not of other proteins including TRP and TRPL, which form the rhabdomeric channels for phototransduction (Niemeyer et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

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The roles of Syx5 in Golgi morphology and Rhodopsin transport inDrosophilaphotoreceptors

Satoh

Nakamura

2016

Biology Open

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SNAREs (SNAP receptors) are the key components of protein complexes that drive membrane fusion. Here, we report the function of a SNARE, Syntaxin 5 (Syx5), in the development of photoreceptors in Drosophila. In wild-type photoreceptors, Syx5 localizes to cis-Golgi, along with cis-Golgi markers: Rab1 and GM130. We observed that Syx5-deficient photoreceptors show notable accumulation of these cis-Golgi markers accompanying drastic accumulation of vesicles between endoplasmic reticulum (ER) and Golgi cisternae. Extensive analysis of Rh1 (rhodopsin 1) trafficking revealed that in Syx5-deficient photoreceptors, Rh1 is exported from the ER with normal kinetics, retained in the cis-Golgi region along with GM130 for a prolonged period, and then subsequently degraded presumably by endoplasmic reticulum-associated protein degradation (ERAD) after retrieval to the ER. Unlike our previous report of Rab6-deficient photoreceptors – where two apical transport pathways are specifically inhibited – vesicle transport pathways to all plasma membrane domains are inhibited in Syx5-deficient photoreceptors, implying that Rab6 and Syx5 are acting in different steps of intra-Golgi transport. These results indicate that Syx5 is crucial for membrane protein transport, presumably during ER-derived vesicle fusion to form cis-Golgi cisternae.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The roles of Syx5 in Golgi morphology and Rhodopsin transport inDrosophilaphotoreceptors

Satoh

Nakamura

2016

Biology Open

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“…GOS-28 is a Golgi SNARE distributed across the Golgi, including the cis-, medial-, and trans-cisterna and that mediates docking and fusion of vesicles from the ER and within the Golgi apparatus [42]. GOS-28 is a type II transmembrane protein that possesses three N-terminal regulatory helical domains of unknown function, a C-terminal SNARE motif, and a transmembrane domain.…”

Section: Gos-28mentioning

confidence: 99%

Caspases rule the intracellular trafficking cartel

2017

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During apoptosis, caspases feast on several hundreds of cellular proteins to orchestrate rapid cellular demise. Indeed, caspases are known to get a taste of every cellular process in one way or another, activating some, but most often shutting them down. Thus, it is not surprising that caspases proteolyze proteins involved in intracellular trafficking with particularly devastating consequences for this important process. This review article focuses on how caspases target the machinery responsible for smuggling goods within and outside the cell.

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“…Maekawa et al reported that GS28 knockout in Caenorhabditis elegans led to a reduction in seam cells and defects in ray formation during development, suggesting that GS28 has roles in cell growth and differentiation. GS28 mutants also show defects in photoreceptor survival in Drosophila …”

Section: Introductionmentioning

confidence: 99%

Role of GS28 in sodium nitroprusside‐induced cell death in cervical carcinoma cells

Rim

Yoo

Lee

et al. 2019

J Biochem & Molecular Tox

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Golgi S‐nitro‐N‐acetylpenicillamine receptor complex 1 (GS28) has been implicated in Golgi vesicle transport. We examined the role of GS28 and its molecular mechanisms in sodium nitroprusside (SNP)‐induced cell death using GS28 siRNA (siGS28)‐transfected HeLa cells. Significant inhibition of cytotoxicity was observed in the cells treated with SNP, and photodegraded SNP showed equal cytotoxicity to SNP. Pretreatment with an ERK inhibitor or siErk1 cotransfection blocked the inhibition in cytotoxicity. Additionally, increased phosphorylation of ERK was maintained in the cells treated with SNP, and Nrf2 level was dependent on ERK phosphorylation. However, pretreatment with a pan‐caspase inhibitor had no effect on cytotoxicity or procaspase‐3 level. Pretreatment with an autophagy inhibitor or siATG5 cotransfection blocked the inhibition of cytotoxicity. The changes of LC3 corresponded to that in siErk1‐cotransfected cells. These data suggest that GS28 has an inductive role in SNP‐induced cell death via inhibition of ERK, leading to inhibition of autophagic processes in HeLa cells.

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The Gos28 SNARE Protein Mediates Intra-Golgi Transport of Rhodopsin and Is Required for Photoreceptor Survival

Cited by 17 publications

References 79 publications

The roles of Syx5 in Golgi morphology and Rhodopsin transport inDrosophilaphotoreceptors

The roles of Syx5 in Golgi morphology and Rhodopsin transport inDrosophilaphotoreceptors

Caspases rule the intracellular trafficking cartel

Role of GS28 in sodium nitroprusside‐induced cell death in cervical carcinoma cells

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