Hm1 muscarinic cholinergic receptor internalization requires a domain in the third cytoplasmic loop.

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Article

Hm1 muscarinic cholinergic receptor internalization requires a domain in the third cytoplasmic loop.

The Journal of biological chemistry - 5 Jul 1992

Lameh J, Philip M, Sharma Y K, Moro O, Ramachandran J, Sadée W

Abstract excerpt

Selected regions of the Hm1 muscarinic cholinergic receptor were mutated to analyze the molecular mechanisms of agonist-induced receptor internalization (or sequestration). The wild-type and mutant Hm1 genes were expressed, using pSG5, in U293 human kidney cells. Whereas surface receptor density measured with the polar tracer N-[3H]methylscopolamine was rapidly reduced by carbachol exposure, total receptor...

Topics

Amino Acid Sequence
Binding Sites
Calcimycin
Carbachol
Cells, Cultured
Cytoplasm
Humans
Kidney
Molecular Sequence Data
Mutation
N-Methylscopolamine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphorylation

Quinuclidinyl Benzilate

Receptors, Muscarinic

Scopolamine Derivatives

Sequence Alignment

Tetradecanoylphorbol Acetate

Transfection

Source

Open in PubMed

Identifiers

PMID: 1618842

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1618842-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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