The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH

Maurer, Meghan E.; Cooper, Jonathan A.

doi:10.1242/jcs.03217

Cited by 200Cellular transport and secretionCholesterol and Lipid MetabolismCaveolin-1 and cellular processes

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The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH

Maurer, Meghan E., Cooper, Jonathan A.·2006·Journal of Cell Science

DOI 10.1242/jcs.03217

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Abstract

Clathrin-mediated endocytosis requires cargo-specific adaptor proteins that recognize specific receptors and recruit them into coated pits. ARH [also called low-density lipoprotein receptor (LDLR) adaptor protein] serves as an adaptor for LDLR endocytosis in liver. However, ARH is dispensable for LDL uptake by some other cell types. Here, we show that the adaptor Dab2 plays a major role in LDLR internalization in HeLa cells and fibroblasts. Dab2 mediates internalization of LDLRs but not transferrin receptors independently of ARH and the classic clathrin adaptor AP-2. If Dab2 is absent, ARH can mediate LDLR endocytosis, but its action requires AP-2. Furthermore, the rate of LDLR endocytosis is decreased when Dab2 is absent and Dab2, but not ARH, catalyzes the efficient clustering of LDLR into coated pits. Dab2 activity requires its binding to clathrin, LDLR and phospholipids. Dab2 is also involved in moving LDLRs off filopodia. We suggest that Dab2 is a cargo-specific endocytic adaptor protein, stably associating with phospholipids and clathrin to sort LDLR to nascent-coated pits, whereas ARH might accelerate later steps in LDLR endocytosis in cooperation with AP-2.

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Changes in LDLR transcription, internalization, stability, subcellular localization, and degradation all affect the concentration of LDL-c in blood.
“Its central role in this process is illustrated by the notion that changes in its transcription, 22 internalization, 23,24 stability, 25 subcellular localization, and degradation 26,27 all affect the concentration of LDL-c in blood.”
From A common variant in CCDC93 protects against myocardial infarction and cardiovascular mortality by regulating endosomal trafficking of low-density lipoprotein receptor (2020) · cites this paper as [23]
Dab2 recruits LDL receptor into clathrin-coated pits and facilitates endocytosis.
“Dab2 is able to recruit LDL receptor into clathrin-coated pits and facilitate endocytosis”
From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Maurer and Cooper, 2006
In cultured cells, Dab2 plays a role in the endocytosis of LDL receptor, in coordination with Arh.
“In studies using cultured cells, Dab2 was found to play a role in the endocytosis of LDL receptor, in coordination with Arh”
From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Maurer and Cooper, 2006
The ARH-NPxY interaction allows binding of AP-2 protein, which recruits additional clathrin, leading to clathrin polymerization and invagination of the plasma membrane to initiate endocytosis.
“This interaction allows binding of the AP-2 protein81, which recruits additional clathrin leading to clathrin polymerization and invagination of the plasma membrane to initiate endocytosis.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [81]
LDLR is translocated to the Golgi network where it is glycosylated and released via vesicles to the plasma membrane, where it is recruited by Dab2 to reside within clathrin-rich pits.
“It is then translocated to the Golgi network where it is glycosylated and released via vesicles to the plasma membrane, where is it recruited by Dab281 to reside within clathrin-rich pits82–84.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [81]

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A Single Common Portal for Clathrin-mediated Endocytosis of Distinct Cargo Governed by Cargo-selective Adaptors
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Authors: Maurer, M. E., & Cooper, J. A.
Affiliations: Fred Hutch Cancer Center (US)
Corresponding author: Cooper, Jonathan A.
ORCID: Cooper, Jonathan A.
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2006-10-15
Volume: 119
Issue: 20
Pages: 4235-4246
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.03217
OpenAlex: W2139362624
Semantic Scholar: 87c9139080b2aa07336baeb4c618e7a82b728533
Cited by: 195
References: 50
Citations by year: 2026: 4 · 2025: 7 · 2024: 5 · 2023: 8 · 2022: 9 · 2021: 8 · 2020: 11 · 2019: 12 · 2018: 5 · 2017: 7 · 2016: 12 · 2015: 13 · 2014: 9 · 2013: 15 · 2012: 9
FWCI: 3.75
Type: journal article
Language: en
Open access: closed
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (R01GM066257, T32GM007270)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords: Dab2, LDL receptor, clathrin-mediated endocytosis, adaptor proteins, AP-2, ArH+, coated pits, receptor internalization, phospholipid binding, filopodia, LDL uptake, transferrin receptor
MeSH terms: Clathrin, Coated Pits, Cell-Membrane, Endocytosis, HeLa Cells, Humans, Models, Biological, Phospholipids, Protein Binding, Receptors, LDL, Myosin Heavy Chains, Gene Silencing, Protein Transport, Tumor Suppressor Proteins, Adaptor Protein Complex 2, RNA, Small Interfering, Transcription Factor TFIIIB, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins

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The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH

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