Reduction in Golgi apparatus dimension in the absence of a residential protein, N-acetylglucosaminyltransferase V

Dong, Zhizhong; Zuber, Christian; Pierce, Michael; Stanley, Pamela; Roth, Jürgen

doi:10.1007/s00418-013-1146-1

Cited by 9 publications

(6 citation statements)

References 108 publications

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“…For example, a mutation in the membrane-spanning domain of an N-acetylglucosaminyltransferase I caused a dramatic effect on Golgi morphology [129]. In CHO cells lacking N-acetylglucosaminyltransferase V (MGAT5), the Golgi volume density was significantly reduced [130]; however, this was not ascribed to the lack of enzymatic function, given that in the absence (or inhibition) of its precursors, MGAT1 and Mann-II, the Golgi seems unaffected. However, we do not rule out that this possibility may be limited only to the glycosyltransferases that form complexes with cytoskeletal proteins [131][132][133].…”

Section: Discussionmentioning

confidence: 99%

Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Frisbie

Lushnikov

Krasnoslobodtsev

et al. 2019

Cells

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Background: The Golgi apparatus undergoes disorganization in response to stress, but it is able to restore compact and perinuclear structure under recovery. This self-organization mechanism is significant for cellular homeostasis, but remains mostly elusive, as does the role of giantin, the largest Golgi matrix dimeric protein. Methods: In HeLa and different prostate cancer cells, we used the model of cellular stress induced by Brefeldin A (BFA). The conformational structure of giantin was assessed by proximity ligation assay and atomic force microscopy. The post-BFA distribution of Golgi resident enzymes was examined by 3D SIM high-resolution microscopy. Results: We detected that giantin is rather flexible than an extended coiled-coil dimer and BFA-induced Golgi disassembly was associated with giantin monomerization. A fusion of the nascent Golgi membranes after BFA washout is forced by giantin re-dimerization via disulfide bond in its luminal domain and assisted by Rab6a GTPase. GM130-GRASP65-dependent enzymes are able to reach the nascent Golgi membranes, while giantin-sensitive enzymes appeared at the Golgi after its complete recovery via direct interaction of their cytoplasmic tail with N-terminus of giantin. Conclusion: Post-stress recovery of Golgi is conducted by giantin dimer and Golgi proteins refill membranes according to their docking affiliation rather than their intra-Golgi location.

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Section: Discussionmentioning

confidence: 99%

Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Frisbie

Lushnikov

Krasnoslobodtsev

et al. 2019

Cells

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“…It can be that the Golgi of a knockout worm is seeking to ‘self-correct’ similarly to the case in glycosylation-defective mammalian cells, where loss of GlcNAc transferase II results in a shift from multiple single LacNAc caps to the expression of longer linear polyLacNAc (53). Also, it can be that lack of a major Golgi enzyme may result in alterations in Golgi morphology as has been reported for the case when GlcNAc transferase V, but not GlcNAc transferase I, is absent from mutant Chinese hamster ovary cells (54). Some of the shifts in the glycome are reflected in the biosynthetic scheme shown in Supplementary Figure 2, whereby the usual core fucosylation events as well as the ability to generate antennae are affected.…”

Section: Discussionmentioning

confidence: 86%

Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans

Yan

Wang

Schachter

et al. 2018

Biochimica et Biophysica Acta (BBA) - General Subjects

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The modification in the Golgi of N-glycans by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1) can be considered to be a hallmark of multicellular eukaryotes as it is found in all metazoans and plants, but rarely in unicellular organisms. The enzyme is key for the normal processing of N-glycans to either complex or paucimannosidic forms, both of which are found in the model nematode Caenorhabditis elegans. Unusually, this organism has three different GlcNAc-TI genes (gly-12, gly-13 and gly-14); therefore, a complete abolition of GlcNAc-TI activity required the generation of a triple knock-out strain. Previously, the compositions of N-glycans from this mutant were described, but no detailed structures. Using an off-line HPLC-MALDI-TOF-MS approach combined with exoglycosidase digestions and MS/MS, we reveal that the multiple hexose residues of the N-glycans of the gly-12;gly-13;gly-14 triple mutant are not just mannose, but include galactoses in three different positions (β-intersecting, β-bisecting and α-terminal) on isomeric forms of HexHexNAc structures; some of these structures are fucosylated and/or methylated. Thus, the N-glycomic repertoire of Caenorhabditis is even wider than expected and exhibits a large degree of plasticity even in the absence of key glycan processing enzymes from the Golgi apparatus.

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“…GMII trims the mannose residue and contributes to the formation of the core GlcNAcMan3GlcNAc2 glycosyl structure, which is a necessary basis for the further adjunction of N-acetyl-glucosamine, and so we took it for granted that the high expression of GMII leads to abnormal N-glycan formation of the glycoproteins. Recently, a study reported that swainsonine can decrease the synthesis of β1,6-branched N-glycans by inhibiting GMII, which means that GMII should participate in the β1,6-branched N-glycan formation 27. In the last years, some studies have pointed that alterations of β1,6-branched of N-glycans were related to proliferation potential, tissue invasion and metastasis, which were recognized as hallmarks of cancer progression 28.…”

Section: Discussionmentioning

confidence: 99%

<p>High expression of GMⅡ is associated with poor prognosis of gastric cancer patients</p>

Zhu

Wei

et al. 2019

OTT

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Background: Being an important N-glycosylation enzyme in eukaryotic cells, Golgi α-mannosidaseⅡ (GMⅡ) has been suggested to function as a target for cancer treatment based on the inhibitory effect on cancer growth and metastasis by the swainsonine, an inhibitor of GMⅡ. This study aims to investigate GMⅡ expression and its prognostic value in primary gastric cancer. Methods: The GMⅡ expression was examined by using the quantitative PCR and Western blotting in 37 paired gastric cancer and noncancerous tissues. We analyzed the relationship between its expression and the clinicopathological parameters by immunohistochemistry in 185 paraffin-embedded gastric cancer tissue specimens. Furthermore, we detected the GMⅡ expression in cultured gastric cancer cell lines and the normal gastric cell line and observed the changes of proliferative and invasive capacities of gastric cell lines after GMⅡ scilencing and overexpressing in vitro. Results: The GMⅡ mRNA ( P <0.0001) and protein ( P <0.01) expression of 37 tumor tissues were increased compared with those of the matched adjacent normal tissues. Human gastric cancer cell lines also showed higher GMⅡ expression ( P <0.001) compared with normal gastric cell lines. The immunohistochemical analysis revealed that GMⅡ was an independent predictor of the overall survival of patients. In addition, GMⅡ overexpression in the normal gastric cell line GES-1 significantly promoted the cell proliferation and invasion, while GMⅡ knockdown in gastric cancer cell line BGC-823 significantly inhibited the cell proliferation and invasion. Conclusion: GMⅡ may become an indicator for monitoring the prognosis of primary gastric cancer and it may provide a new direction for precise treatment.

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Reduction in Golgi apparatus dimension in the absence of a residential protein, N-acetylglucosaminyltransferase V

Cited by 9 publications

References 108 publications

Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans

<p>High expression of GMⅡ is associated with poor prognosis of gastric cancer patients</p>

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