Targeting of proteins to the Golgi apparatus

Gleeson, Paul A.; Teasdale, Rohan D.; Burke, Jo

doi:10.1007/bf00731273

Cited by 79 publications

(79 citation statements)

References 124 publications

(114 reference statements)

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“…We also addressed their trafficking and suggested recycling between the ER and Golgi to ascertain whether the observed complexes are compatible with the preferred "cisternal progression" or "rapid partitioning" Golgi trafficking models, both of which implicate that Golgi enzymes are mobile membrane constituents that continuously recycle between the Golgi and the ER (26 -30). In contrast, the "stable compartments" model assumes that oligomerization results in stable enzyme assemblies that are physically too large to fit into post-Golgi transport vesicles (31)(32)(33)(34). Our results show that the Golgi glycosyltransferase homomers and heteromers are interdependent and mobile membrane constituents that are assembled in the ER and the Golgi, respectively, and that undergo dynamic organellar microenvironment-dependent transitions between these two physical states during their recycling between the Golgi and the ER.…”

mentioning

confidence: 74%

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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mentioning

confidence: 74%

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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“…pECFP-Golgi encodes a fusion protein consisting of ECFP and a sequence encoding the N-terminal 81 amino acids of human ␤-1,4-galactosyltransferase (50). This region of human ␤-1,4-galactosyltransferase contains the membrane-anchoring signal peptide that targets the fusion protein to the transmedial region of the Golgi apparatus (24,34,52). pECFP-Endo encodes a fusion protein consisting of the human RhoB 4 cells) and 7 l of the pelleted supernatant (corresponding to 3.5 ϫ 10 5 cells) were separated by SDS-12% polyacrylamide gel electrophoresis and electrophoretically transferred onto polyvinylidene fluoride membranes.…”

Section: Methodsmentioning

confidence: 99%

Multivesicular Bodies as a Platform for Formation of the Marburg Virus Envelope

Kolesnikova

Berghöfer

Bamberg

et al. 2004

J Virol

101

124

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The Marburg virus (MARV) envelope consists of a lipid membrane and two major proteins, the matrix protein VP40 and the glycoprotein GP. Both proteins use different intracellular transport pathways: GP utilizes the exocytotic pathway, while VP40 is transported through the retrograde late endosomal pathway. It is currently unknown where the proteins combine to form the viral envelope. In the present study, we identified the intracellular site where the two major envelope proteins of MARV come together as peripheral multivesicular bodies (MVBs). Upon coexpression with VP40, GP is redistributed from the trans-Golgi network into the VP40-containing MVBs. Ultrastructural analysis of MVBs suggested that they provide the platform for the formation of membrane structures that bud as virus-like particles from the cell surface. The virus-like particles contain both VP40 and GP. Single expression of GP also resulted in the release of particles, which are round or pleomorphic. Single expression of VP40 led to the release of filamentous structures that closely resemble viral particles and contain traces of endosomal marker proteins. This finding indicated a central role of VP40 in the formation of the filamentous structure of MARV particles, which is similar to the role of the related Ebola virusVP40. In MARV-infected cells, VP40 and GP are colocalized in peripheral MVBs as well. Moreover, intracellular budding of progeny virions into MVBs was frequently detected. Taken together, these results demonstrate an intracellular intersection between GP and VP40 pathways and suggest a crucial role of the late endosomal compartment for the formation of the viral envelope.

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“…The Golgi marker vector (pEGFP-Golgi) was constructed using the pECFP-Golgi vector (Clontech) that harbors a sequence encoding the N-terminal 81 amino acids of human ␤1-4-galactosyltransferase (24). This region of human ␤1-4-galactosyltransferase contains the membrane-anchoring signal peptide that targets the fusion protein to the trans-medial region of the Golgi apparatus (25)(26)(27). The region from pECFP-Golgi was digested with NheI and BamHI and subcloned into pEGFP-N1.…”

Section: Expression Of a Soluble Form Of Csglca-t (Chsy-3)mentioning

confidence: 99%

Identification of Chondroitin Sulfate Glucuronyltransferase as Chondroitin Synthase-3 Involved in Chondroitin Polymerization

Izumikawa

Koike

Shiozawa

et al. 2008

Journal of Biological Chemistry

128

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Recently, we demonstrated that chondroitin polymerization is achieved by any two combinations of human chondroitin synthase-1 (ChSy-1), ChSy-2 (chondroitin sulfate synthase 3, CSS3), and chondroitin-polymerizing factor (ChPF). Although an additional ChSy family member, called chondroitin sulfate glucuronyltransferase (CSGlcA-T), has been identified, its involvement in chondroitin polymerization remains unclear because it possesses only glucuronyltransferase II activity responsible for the elongation of chondroitin sulfate (CS) chains. Herein, we report that CSGlcA-T exhibits polymerization activity on ␣-thrombomodulin bearing the truncated linkage region tetrasaccharide through its interaction with ChSy-1, ChSy-2 (CSS3), or ChPF, and the chain length of chondroitin formed by the co-expressed proteins in various combinations is different. In addition, ChSy family members co-expressed in various combinations exhibited distinct but overlapping acceptor substrate specificities toward the two synthetic acceptor substrates, GlcUA␤1-3Gal␤1-O-naphthalenemethanol and GlcUA␤1-3Gal␤1-O-C 2 H 4 NH-benzyloxycarbonyl, both of which share the disaccharide sequence with the glycosaminoglycan-protein linkage region tetrasaccharide. Moreover, overexpression of CSGlcA-T increased the amount of CS in HeLa cells, whereas the RNA interference of CSGlcA-T resulted in a reduction of the amount of CS in the cells. Furthermore, the analysis using the CSGlcA-T mutant that lacks any glycosyltransferase activity but interacts with other ChSy family members showed that the glycosyltransferase activity of CSGlcA-T plays an important role in chondroitin polymerization. Overall, these results suggest that chondroitin polymerization is achieved by multiple combinations of ChSy-1, ChSy-2, CSGlcA-T, and ChPF and that each combination may play a unique role in the biosynthesis of CS. Based on these results, we renamed CSGlcA-T chondroitin synthase-3 (ChSy-3).

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Targeting of proteins to the Golgi apparatus

Cited by 79 publications

References 124 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

Multivesicular Bodies as a Platform for Formation of the Marburg Virus Envelope

Identification of Chondroitin Sulfate Glucuronyltransferase as Chondroitin Synthase-3 Involved in Chondroitin Polymerization

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