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Domain map of the LDL receptor: Sequence homology with the epidermal growth factor precursor

Russell, David W., Schneider, Wolfgang J., Yamamoto, Tokuo, Luskey, Kenneth L., Brown, Michael S., Goldstein, Joseph L.·1984·Cell
DOI 10.1016/0092-8674(84)90388-x
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Abstract

The nucleotide sequence of a partial cDNA for the bovine low-density lipoprotein (LDL) receptor revealed an open reading frame of 264 amino acids that encodes the COOH-terminal 25% of the receptor protein. The sequence predicts a cytoplasmic domain of 50 amino acids at the COOH terminus, followed in order by a membrane-spanning region of 27 hydrophobic amino acids and an externally disposed stretch of 42 amino acids, that is rich in serine and threonine residues and appears to be the site of O-linked glycosylation. This orientation was confirmed by proteolysis experiments in which the relevant fragments were localized by blotting with anti-peptide antibodies and a galactose-specific lectin. The extracytoplasmic domain of the LDL receptor contains a region that is 38% identical with a 96 amino acid sequence in the precursor to mouse epidermal growth factor (EGF), a peptide hormone. This unexpected homology raises the possibility that proteins involved in growth stimulation (e.g., EGF precursor) and nutrient delivery (e.g., LDL receptor) may have a common evolutionary origin.

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  • LDLR is a type I membrane protein with an extracellular/luminal N-terminus, a single transmembrane helix, and a cytosolic C-terminus.

    “LDLR is a type I membrane protein, meaning that it possesses an extracellular/luminal N-terminus, followed by a single transmembrane helix and a cytosolic C-terminus, such that this integral membrane protein spans the entirety of the cell membrane11–13.”

    From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [11]

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Metadata

Authors
Russell, D. W., Schneider, W. J., Yamamoto, T., Luskey, K. L., Brown, M. S., & Goldstein, J. L.
Venue
Cell
Publisher
Elsevier BV
Published
1984-06
Volume
37
Issue
2
Pages
577-585
ISSN
0092-8674
DOI
10.1016/0092-8674(84)90388-x
Cited by
282
References
0
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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