ArticleThe EMBO journal1991
Sequences within and adjacent to the transmembrane segment of alpha-2,6-sialyltransferase specify Golgi retention.
Article in The EMBO journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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Who cites it
114 citing papers in PubMed, 296 citations in OpenAlex.
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- Dynamic movement of the Golgi unit and its glycosylation enzyme zones.Nature communications · 2024Article
- Sorting of secretory proteins at theeLife · 2024Article
- Downregulation of endogenous nectin1 in human keratinocytes by herpes simplex virus 1 glycoprotein D excludes superinfection but does not affect NK cell function.The Journal of general virology · 2024Article
- Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation.Cells · 2021Review
- GOLPH3 and GOLPH3L are broad-spectrum COPI adaptors for sorting into intra-Golgi transport vesicles.The Journal of cell biology · 2021Article
- Direct trafficking pathways from the Golgi apparatus to the plasma membrane.Seminars in cell & developmental biology · 2020Review
- The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation.The Journal of biological chemistry · 2020Article
- Reconstruction of the sialylation pathway in the ancestor of eukaryotes.Scientific reports · 2018Article
- Article
- A role for Sar1 and ARF1 GTPases during Golgi biogenesis in the protozoan parasiteMolecular biology of the cell · 2017Article
- Sialylation of N-glycans: mechanism, cellular compartmentalization and function.Histochemistry and cell biology · 2017Review
- Evolution of protein N-glycosylation process in Golgi apparatus which shapes diversity of protein N-glycan structures in plants, animals and fungi.Scientific reports · 2017Article
- Transmembrane Domain Lengths Serve as Signatures of Organismal Complexity and Viral Transport Mechanisms.Scientific reports · 2016Article
- Contributions of epsinR and gadkin to clathrin-mediated intracellular trafficking.Molecular biology of the cell · 2015Article
- Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.Nature communications · 2015Article
- Organization and dynamics of SNARE proteins in the presynaptic membrane.Frontiers in physiology · 2015Review
- Golgi phosphoprotein 3 triggers signal-mediated incorporation of glycosyltransferases into coatomer-coated (COPI) vesicles.The Journal of biological chemistry · 2014Article
- A versatile system for USER cloning-based assembly of expression vectors for mammalian cell engineering.PloS one · 2014Article
- Anchors aweigh: protein localization and transport mediated by transmembrane domains.Trends in cell biology · 2013Review
54 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycosyltransferase alpha-2,6-sialyltransferase (ST) is a Type II membrane protein localized to the Golgi apparatus. The first 44 amino acids of this protein were able to specify Golgi retention of a fused marker protein, lysozyme. This section of ST contains a transmembrane segment which serves as a non-cleaved signal anchor. When lysozyme was fused to an equivalent region of a cell surface protein it now appeared on the cell surface. Analysis of chimeras between the two proteins revealed that the transmembrane segment of ST specifies Golgi retention. Furthermore, altering this segment in full-length ST results in the protein accumulating on the cell surface. However, the retaining effect of the transmembrane domain of ST is augmented by the presence of adjacent lumenal and cytoplasmic sequences from ST. If these sequences are spaced apart by a transmembrane domain of the same length as that of ST they too can specify Golgi retention. Thus retention in the Golgi of ST appears to involve recognition of an extended region of the protein within and on both sides of the bilayer.
Indexed as
Identifiers
1935890PMC453089W270749527What OpenQuestion holds
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.