Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 3 (bis 2014)- Genetics (C. Nüsslein-Volhard)     Display Documents



  history
ID: 705437.0, MPI für Entwicklungsbiologie / Abteilung 3 (bis 2014)- Genetics (C. Nüsslein-Volhard)
The glucosyltransferase Xiantuan of the endoplasmic reticulum specifically affects E-Cadherin expression and is required for gastrulation movements in Drosophila
Authors:Zhang, Y.; Kong, D.; Reichl, L.; Vogt, N.; Wolf, F.; Grosshans, J.
Language:English
Date of Publication (YYYY-MM-DD):2014-06-15
Title of Journal:Developmental Biology
Journal Abbrev.:Dev Biol
Volume:390
Issue / Number:2
Start Page:208
End Page:220
Sequence Number of Article:24681004
Review Status:Internal review
Audience:Experts Only
Abstract / Description:The majority of membrane and secreted proteins, including many developmentally important signalling proteins, receptors and adhesion molecules, are cotranslationally N-glycosylated in the endoplasmic reticulum. The structure of the N-glycan is invariant for all substrates and conserved in eukaryotes. Correspondingly, the enzymes are conserved, which successively assemble the glycan precursor from activated monosaccharides prior to transfer to nascent proteins. Despite the well-defined biochemistry, the physiological and developmental role of N-glycosylation and of the responsible enzymes has not been much investigated in metazoa. We identified a mutation in the Drosophila gene, xiantuan (xit, CG4542), which encodes one of the conserved enzymes involved in addition of the terminal glucose residues to the glycan precursor. xit is required for timely apical constriction of mesoderm precursor cells and ventral furrow formation in early embryogenesis. Furthermore, cell intercalation in the lateral epidermis during germband extension is impaired in xit mutants. xit affects glycosylation and intracellular distribution of E-Cadherin, albeit not the total amount of E-Cadherin protein. As depletion of E-Cadherin by RNAi induces a similar cell intercalation defect, E-Cadherin may be the major xit target that is functionally relevant for germband extension.
Free Keywords:Adherens Junctions/physiology; Animals; Base Sequence; Blotting, Western; Cadherins/*metabolism; Drosophila/*embryology/enzymology; Drosophila Proteins/genetics/*metabolism; Endoplasmic Reticulum/*metabolism; Fluorescence; Gastrulation/*physiology; Gene Components; Gene Expression Regulation/genetics/*physiology; Glucosyltransferases/genetics/*metabolism; Microscopy, Confocal; Molecular Sequence Data; Movement/*physiology; RNA Interference; Sequence Analysis, DNA
External Publication Status:published
Document Type:Article
Communicated by:MPI für Entwickungsbiologie
Affiliations:MPI für Entwicklungsbiologie/Abteilung 3 - Genetik (Christiane Nüsslein-Volhard)
External Affiliations:Max-Planck-Institut fur Dynamik und Selbstorganisation, Am Fassberg 17, 37077 Gottingen, Germany. Max-Planck-Institut fur Entwicklungsbiologie, Spemannstrasse 35, 72072 Tubingen, Germany. Institut fur Entwicklungsbiochemie, Universitatsmedizin, Universitat Gottingen, Justus-Liebig Weg 11, 37077 Gottingen, Germany. Electronic address: jgrossh@gwdg.de.
Identifiers:ISSN:1095-564X (Electronic) 0012-1606 (Linking) %R 10.1... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/pubmed/24681004 [ID No:2]
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.