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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Giantin-knockout models reveal a feedback loop between Golgi function and glycosyltransferase expression.

Nicola L Stevenson1, Dylan J M Bergen1,2, Roderick E H Skinner2

  • 1Cell Biology Laboratories, School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.

Journal of Cell Science
|November 3, 2017
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Summary

Giantin, a key Golgi protein, regulates gene expression, particularly glycosyltransferases like GALNT3. Its absence causes disease-like symptoms in zebrafish, revealing Golgi’s role in maintaining proteoglycome homeostasis.

Keywords:
GALNT3GiantinGlycosylationGolgiHyperphosphatemic tumoral calcinosisZebrafish

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The Golgi apparatus is crucial for complex glycosylation, protein modification, and cellular organization.
  • Golgins are essential structural proteins that organize Golgi cisternae and vesicle transport.
  • Giantin is the largest known golgin, implicated in Golgi structure and function.

Purpose of the Study:

  • To investigate the role of giantin in Golgi homeostasis and gene expression.
  • To determine the impact of giantin ablation on glycosylation pathways.
  • To explore the physiological consequences of giantin loss in cellular and organismal models.

Main Methods:

  • Gene knockout of giantin in mammalian cells and zebrafish.
  • Analysis of gene expression profiles using transcriptomics.
  • Assessment of Golgi structure and glycosyltransferase activity.
  • Phenotypic analysis of giantin-knockout zebrafish.

Main Results:

  • Giantin knockout caused significant changes in gene expression, affecting 22 Golgi-resident glycosyltransferases.
  • GALNT3 function was nearly abolished in giantin-deficient cells and zebrafish.
  • Giantin-knockout zebrafish displayed hyperostosis and ectopic calcification, mimicking human diseases linked to GALNT3 mutations.
  • Golgi structure showed limited alterations, suggesting a primary role in regulating gene expression rather than organization.

Conclusions:

  • Giantin plays a critical role in regulating the expression of Golgi-resident glycosyltransferases, impacting proteoglycome synthesis.
  • Dysregulation of GALNT3 due to giantin loss contributes to pathological calcification.
  • These findings highlight a novel mechanism of Golgi homeostasis involving the control of glycosyltransferase expression.