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Article

A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin.

The Journal of cell biology - 1 Aug 1991

Brewer C B, Roth M G

Abstract excerpt

In the polarized kidney cell line MDCK, the influenza virus hemagglutinin (HA) has been well characterized as a model for apically sorted membrane glycoproteins. Previous work from our laboratory has shown that a single amino acid change in the cytoplasmic sequence of HA converts it from a protein that is excluded from coated pits to one that is efficiently internalized. Using trypsin or antibodies to mark...

Topics

Animals
Antibodies
Biological Transport
Cell Line
Cytoplasm
Endocytosis
Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral
Kinetics
Methionine
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Precipitin Tests

Transfection

Transferrin

Trypsin

Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 1860878
DOI: 10.1083/jcb.114.3.413
PMCID: PMC2289095

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1860878-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin.PMID 1860878Read ↗

Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL.Semantic proximity Read ↗

Endocytosis of chimeric influenza virus hemagglutinin proteins that lack a cytoplasmic recognition feature for coated pits.Semantic proximity Read ↗

Apical budding of a recombinant influenza A virus expressing a hemagglutinin protein with a basolateral localization signal.Semantic proximity Read ↗

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Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi.Semantic proximity Read ↗

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Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis.Semantic proximity Read ↗

An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells.Semantic proximity Read ↗

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