Models for Golgi Traffic: A Critical Assessment

Glick, Benjamin S.; Luini, Alberto

doi:10.1101/cshperspect.a005215

Cited by 191 publications

(192 citation statements)

References 89 publications

(155 reference statements)

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“…Thus, complex formation itself appears to neither restrict intra-Golgi transport nor their recycling between the Golgi and the ER. Therefore, the formation of glycosyltransferase complexes is fully compatible with the "cisternal maturation" or the "rapid partitioning" models, which both entail that the cisternal contents change both laterally and along the cis-trans axis of the Golgi stack (29,30,50,51). The data are also compatible with the suggested recycling of the Golgi glycosyltransferases between the Golgi and the ER (42).…”

Section: Discussionsupporting

confidence: 76%

Organizational Interplay of Golgi N-Glycosyltransferases Involves Organelle Microenvironment-Dependent Transitions between Enzyme Homo- and Heteromers

Hassinen

Kellokumpu

2014

Journal of Biological Chemistry

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Background: Glycans are synthesized in the Golgi by glycosyltransferase complexes, but their functional organization is unclear. Results: Organizational interplay and trafficking of glycosyltransferase complexes involves dynamic transitions between enzyme homo-and heteromers. Conclusion: Organellar microenvironmental factors play a crucial role in the functional organization of the Golgi glycosylation pathways. Significance: Organizational interplay between glycosyltransferase complexes provides new insights into glycosylation and associated diseases.

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Section: Discussionsupporting

confidence: 76%

Organizational Interplay of Golgi N-Glycosyltransferases Involves Organelle Microenvironment-Dependent Transitions between Enzyme Homo- and Heteromers

Hassinen

Kellokumpu

2014

Journal of Biological Chemistry

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“…There are two likely possibilities based on the current models of intra-Golgi transport (14). One model proposes that cargo moves across the Golgi complex via vesicular transport carriers in a cis to trans direction, with the Golgi-resident enzymes remaining in specific cisternae where they function.…”

Section: Discussionmentioning

confidence: 99%

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ

Meel

Qian

Kornfeld

2014

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

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The lysosomal storage disorder mucolipidosis III αβ is caused by mutations in the αβ subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (phosphotransferase). This Golgi-localized enzyme mediates the first step in the synthesis of the mannose 6-phosphate recognition marker on lysosomal acid hydrolases, and loss of function results in impaired lysosomal targeting of these acid hydrolases and decreased lysosomal degradation. Here we show that two patient missense mutations, Lys4Gln and Ser15Tyr, in the N-terminal cytoplasmic tail of the α subunit of phosphotransferase impair retention of the catalytically active enzyme in the Golgi complex. This results in mistargeting of the mutant phosphotransferases to lysosomes, where they are degraded, or to the cell surface and release into the medium. The finding that mislocalization of active phosphotransferase is the basis for mucolipidosis III αβ in a subset of patients shows the importance of single residues in the cytoplasmic tail of a Golgi-resident protein for localization to this compartment.

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“…Indeed, the cisternal maturation in yeast is strictly controlled by COPI, again supporting the main frame of the model (Ishii et al, 2016;Papanikou et al, 2015). It should also be noticed, however, that tubular extensions and interconnections can also play roles in intra-Golgi transport (Glick and Luini, 2011;Glick and Nakano, 2009). …”

Section: Introductionmentioning

confidence: 98%

A Missense Mutation in the <i>NSF</i> Gene Causes Abnormal Golgi Morphology in <i>Arabidopsis thaliana</i>

Tanabashi

Shoda

Saito

et al. 2018

Cell Struct. Funct.

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The Golgi apparatus is a key station of glycosylation and membrane traffic. It consists of stacked cisternae in most eukaryotes. However, the mechanisms how the Golgi stacks are formed and maintained are still obscure. The model plant Arabidopsis thaliana provides a nice system to observe Golgi structures by light microscopy, because the Golgi in A. thaliana is in the form of mini-stacks that are distributed throughout the cytoplasm. To obtain a clue to understand the molecular basis of Golgi morphology, we took a forward-genetic approach to isolate A. thaliana mutants that show abnormal structures of the Golgi under a confocal microscope. In the present report, we describe characterization of one of such mutants, named #46-3. The #46-3 mutant showed pleiotropic Golgi phenotypes. The Golgi size was in majority smaller than the wild type, but varied from very small ones, sometimes without clear association of cis and trans cisternae, to abnormally large ones under a confocal microscope.At the ultrastructual level by electron microscopy, queer-shaped large Golgi stacks were occasionally observed. By positional mapping, genome sequencing, and complementation and allelism tests, we linked the mutant phenotype to the missense mutation D374N in the NSF gene, encoding the N-ethylmaleimide-sensitive factor (NSF), a key component of membrane fusion. This residue is near the ATP-binding site of NSF, which is very well conserved in eukaryotes, suggesting that the biochemical function of NSF is important for maintaining the normal morphology of the Golgi.3

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Models for Golgi Traffic: A Critical Assessment

Cited by 191 publications

References 89 publications

Organizational Interplay of Golgi N-Glycosyltransferases Involves Organelle Microenvironment-Dependent Transitions between Enzyme Homo- and Heteromers

Organizational Interplay of Golgi N-Glycosyltransferases Involves Organelle Microenvironment-Dependent Transitions between Enzyme Homo- and Heteromers

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ

A Missense Mutation in the <i>NSF</i> Gene Causes Abnormal Golgi Morphology in <i>Arabidopsis thaliana</i>

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