ArticleThe Journal of biological chemistry2014
Organizational interplay of Golgi N-glycosyltransferases involves organelle microenvironment-dependent transitions between enzyme homo- and heteromers.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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Who cites it
30 citing papers in PubMed, 55 citations in OpenAlex.
- Endothelial cells sialylate IgG within the FcRn-mediated recycling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Posttranslational sialylation and its impact on neutrophil recruitment.Journal of leukocyte biology · 2025Review
- Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025Review
- Golgi pH homeostasis stabilizes the lysosomal membrane throughLife science alliance · 2024Article
- Unraveling the Intricate Link: Deciphering the Role of the Golgi Apparatus in Breast Cancer Progression.International journal of molecular sciences · 2023Review
- Article
- The tobacco GNTI stem region harbors a strong motif for homomeric protein complex formation.Frontiers in plant science · 2023Article
- Structure of the human heparan sulfate polymerase complex EXT1-EXT2.Nature communications · 2022Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- Fluorescence Lifetime Imaging of pH along the Secretory Pathway.ACS chemical biology · 2022Article
- β-1,4-Xylan backbone synthesis in higher plants: How complex can it be?Frontiers in plant science · 2022Article
- N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome.Experientia supplementum (2012) · 2021Review
- Can endolysosomal deacidification and inhibition of autophagy prevent severe COVID-19?Life sciences · 2020Review
- N-glycosylation of the human β1,4-galactosyltransferase 4 is crucial for its activity and Golgi localization.Glycoconjugate journal · 2020Article
- Sugary Logistics Gone Wrong: Membrane Trafficking and Congenital Disorders of Glycosylation.International journal of molecular sciences · 2020Review
- Assembly of B4GALT1/ST6GAL1 heteromers in the Golgi membranes involves lateral interactions via highly charged surface domains.The Journal of biological chemistry · 2019Article
- A Golgi-associated redox switch regulates catalytic activation and cooperative functioning of ST6Gal-I with B4GalT-I.Redox biology · 2019Article
- N-acetylglucosaminyltransferases and nucleotide sugar transporters form multi-enzyme-multi-transporter assemblies in golgi membranes in vivo.Cellular and molecular life sciences : CMLS · 2019Article
- Golgi pH, Ion and Redox Homeostasis: How Much Do They Really Matter?Frontiers in cell and developmental biology · 2019Article
- Intermediate compartment (IC): from pre-Golgi vacuoles to a semi-autonomous membrane system.Histochemistry and cell biology · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation of proteins and lipids takes place in the Golgi apparatus by the consecutive actions of functionally distinct glycosidases and glycosyltransferases. Current evidence indicates that they function as enzyme homomers and/or heteromers in the living cell. Here we investigate their organizational interplay and show that glycosyltransferase homomers are assembled in the endoplasmic reticulum. Upon transport to the Golgi, the majority of homomers are disassembled to allow the formation of enzyme heteromers between sequentially acting medial-Golgi enzymes GnT-I and GnT-II or trans-Golgi enzymes GalT-I and ST6Gal-I. This transition is driven by the acidic Golgi environment, as it was markedly inhibited by raising Golgi luminal pH with chloroquine. Our FRAP (fluorescence recovery after photobleaching) measurements showed that the complexes remain mobile Golgi membrane constituents that can relocate to the endoplasmic reticulum or to the scattered Golgi mini-stacks upon brefeldin A or nocodazole treatment, respectively. During this relocation, heteromers undergo a reverse transition back to enzyme homomers. These data unveil an unprecedented organizational interplay between Golgi N-glycosyltransferases that involves dynamic and organelle microenvironment-driven transitions between enzyme homomers and heteromers during their trafficking within the early secretory compartments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.