Incorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein
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Summary
The membrane-spanning domain of the vesicular stomatitis virus glycoprotein (G protein) consists of a continuous stretch of 20 uncharged and mostly hydrophobic amino acids and the effects of two mutations which change the amino acid sequence in this domain were examined.
- Type
- article
- Published
- 1985-06-01
- Cited by
- 73
- References
- 25
- Access
- Open access
- OpenAlex
- https://openalex.org/W1884610191
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:37177345
Keywords
Biology, Vesicle-associated membrane protein 8, Vesicular stomatitis virus, Biochemistry, Palmitoylation
References
- Fatty acid acylation of eucaryotic cell membrane proteins
- Vesicular stomatitis virus glycoprotein is anchored to intracellular membranes near its carboxyl end and is proteolytically cleaved at its amino terminus
- Expression of a recombinant DNA gene coding for the vesicular stomatitis virus nucleocapsid protein
- Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions
- A simple method for displaying the hydropathic character of a protein.
- The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition.
- Altered cytoplasmic domains affect intracellular transport of the vesicular stomatitis virus glycoprotein.
- Bacteriorhodopsin is an inside-out protein.
- Mechanisms for the incorporation of proteins in membranes and organelles
- Membrane assembly in vitro: synthesis, glycosylation, and asymmetric insertion of a transmembrane protein.
- Conversion of a secretory protein into a transmembrane protein results in its transport to the Golgi complex but not to the cell surface.
- Intracellular protein topogenesis.
- The hydrophobic effect and the organization of living matter.
- Three-dimensional model of purple membrane obtained by electron microscopy
- Perturbation of vesicular traffic with the carboxylic ionophore monensin.
- Fatty acid binding to vesicular stomatitis virus glycoprotein: a new type of post-translational modification of the viral glycoprotein.
- Synchronised transmembrane insertion and glycosylation of a nascent membrane protein
- SV40-transformed simian cells support the replication of early SV40 mutants.
- Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells.
- Subcellular compartmentalization of saccharide moieties in cultured normal and malignant cells
Cited by
- The semiotics of charge
- Analysis of progressive deletions of the transmembrane and cytoplasmic domains of influenza hemagglutinin
- Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator.
- Vaccinia virus hemagglutinin.
- Reconstitution and physiological protein translocation processes.
- Intracellular transport and functions of mammalian lysosomal membrane glycoproteins
- A patient with type 2N von Willebrand disease is heterozygous for a new mutation: Gly22Glu. Demonstration of a defective expression of the second allele by the use of monoclonal antibodies.
- Domains of Virus Glycoproteins
- Growth factor receptors.
- Virally Infected Cells
- Artificial and Reconstituted Membrane Systems
- High Level Production of Glycoprotein H of HSV-1 (F) Using HcNPV Vector System
- In vitro mutagenesis of the putative membrane-binding domain of polyomavirus middle-T antigen
- Identification and characterization of a human cytomegalovirus gene coding for a membrane protein that is conserved among human herpesviruses
- Cell surface expression and orientation in membranes of the 44-amino-acid SH protein of simian virus 5
- The rat neutrophil low-affinity Fc receptor for IgG: molecular cloning and functional characterization.
- Defective assembly and intracellular transport of mutant paramyxovirus hemagglutinin-neuraminidase proteins containing altered cytoplasmic domains
- The carboxy terminus of human immunodeficiency virus type 1 gp160 limits its proteolytic processing and transport in transfected cell lines
- Variants of vaccinia virus hemagglutinin altered in intracellular transport
- Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane [published erratum appers in J Cell Biol 1988 Jan;106(1):325]
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