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Type II Transforming Growth Factor-β Receptor Recycling Is Dependent upon the Clathrin Adaptor Protein Dab2

Penheiter, Sumedha G., Deep Singh, Raman, Repellin, Claire E., Wilkes, Mark C., Edens, Maryanne, Howe, Philip H., Pagano, Richard E., Leof, Edward B.·2010·Molecular Biology of the Cell
DOI 10.1091/mbc.e09-12-1019PMC PMC2982134
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Abstract

Transforming growth factor (TGF)-β family proteins form heteromeric complexes with transmembrane serine/threonine kinases referred to as type I and type II receptors. Ligand binding initiates a signaling cascade that generates a variety of cell type-specific phenotypes. Whereas numerous studies have investigated the regulatory activities controlling TGF-β signaling, there is relatively little information addressing the endocytic and trafficking itinerary of TGF-β receptor subunits. In the current study we have investigated the role of the clathrin-associated sorting protein Disabled-2 (Dab2) in TGF-β receptor endocytosis. Although small interfering RNA-mediated Dab2 knockdown had no affect on the internalization of various clathrin-dependent (i.e., TGF-β, low-density lipoprotein, or transferrin) or -independent (i.e., LacCer) cargo, TGF-β receptor recycling was abrogated. Loss of Dab2 resulted in enlarged early endosomal antigen 1-positive endosomes, reflecting the inability of cargo to traffic from the early endosome to the endosomal recycling compartment and, as documented previously, diminished Smad2 phosphorylation. The results support a model whereby Dab2 acts as a multifunctional adaptor in mesenchymal cells required for TGF-β receptor recycling as well as Smad2 phosphorylation.

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  • Dab2 facilitates cellular endocytosis and trafficking of TGF-beta receptor.

    “Another study indicates that Dab2 facilitates the cellular endocytosis and trafficking of TGF-beta receptor (Penheiter et al., 2010).”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Penheiter et al., 2010

    The Introduction reports that Dab2 knockdown disrupts TGF-β receptor recycling and endosomal trafficking, supporting the trafficking part of the claim. It also states that knockdown does not affect receptor internalization; the Discussion likewise reports no effect on TGF-β receptor internalization. Thus the paper does not support saying Dab2 facilitates the receptor's initial endocytosis. (LLM, conf=0.92)

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Metadata

Authors
Penheiter, S. G., Deep Singh, R., Repellin, C. E., Wilkes, M. C., Edens, M., Howe, P. H., Pagano, R. E., & Leof, E. B.
Affiliations
  • *Thoracic Diseases Research Unit, Department of Biochemistry and Molecular Biology and Mayo Clinic Cancer Center, Mayo Clinic, Rochester, MN 55905; and
  • Department of Cancer Biology, The Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2010-11-15
Volume
21
Issue
22
Pages
4009-4019
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e09-12-1019
PMC
PMC2982134
Cited by
57
References
4
Language
en

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