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Cited by 506

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Receptor-mediated endocytosis: insights from the lipoprotein receptor system

Brown, M S, Goldstein, J L·1979·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.76.7.3330
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Abstract

The low density lipoprotein (LDL) receptor system coordinates the metabolism of cholesterol, an essential component of the plasma membrane of all mammalian cells. Study of this system has led to an enhanced understanding of the cellular basis of cholesterol homeostasis. It has also brought into focus an important mechanism of metabolic regulation--the process of receptor-mediated endocytosis. In this article, we first describe the receptor-mediated endocytosis of LDL, a sequence of events in which receptor binding and internalization are coupled in specialized regions of the plasma membrane called coated pits. Second, we trace the cellular functions of the cholesterol derived from internalized LDL. Third, genetic evidence is presented to indicate that both the binding and internalization of LDL are mediated by a single receptor molecule that contains two active sites, one mediating binding and the other internalization. Finally, the characteristics of the LDL receptor system are used to suggest models for receptor systems in general.

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Crossref · 10.1073/pnas.76.7.3330

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  • The receptors for LDL (LDLR) and transferrin receptor (TFR) are both endocytosed from the cell surface via clathrin-coated vesicles and transported through intracellular recycling pathways.

    “The receptors for LDL (LDLR) and transferrin receptor (TFR) are both endocytosed from the cell surface via clathrin-coated vesicles and transported through intracellular recycling pathways (14, 15, 16, 17, 18, 19, 20).”

    From The small GTPase RAB10 regulates endosomal recycling of the LDL receptor and transferrin receptor in hepatocytes (2022) · cites this paper as [16]

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Metadata

Authors
Brown, M. S., & Goldstein, J. L.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1979-07
Volume
76
Issue
7
Pages
3330-3337
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.76.7.3330
Cited by
506
References
0
Language
en

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