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PMID: 3494949 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region.

Nature ·Vol. 326 ·No. 6115 ·1987-00-00 ·Pages 760-5

Davis CG, Goldstein JL, Südhof TC, Anderson RG, Russell DW, Brown MS

Abstract

A domain in the low-density lipoprotein receptor contains three cysteine-rich 'growth factor' repeats like those that occur in many proteins. When this domain is deleted, the receptor no longer releases its ligand at acid pH, it is no longer recycled efficiently and it is rapidly degraded after ligand binding.

MeSH Terms

Amino Acid Sequence Animals Base Sequence Chromosome Deletion Cricetinae Cricetulus Cysteine/analysis Epidermal Growth Factor/analysis,genetics Hydrogen-Ion Concentration Lipoproteins, LDL/metabolism Lipoproteins, VLDL/metabolism Plasmids Protein Precursors/analysis,genetics Receptors, LDL/genetics,physiology Repetitive Sequences, Nucleic Acid Structure-Activity Relationship

Chemicals

Lipoproteins, LDL Lipoproteins, VLDL Protein Precursors Receptors, LDL Epidermal Growth Factor Cysteine

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Davis C G

Goldstein J L

Südhof T C

Anderson R G

Russell D W

Brown M S

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/326760a0

Published

1987-00-00

Pages

760-5

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/326760a0 View journal details

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Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region.

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