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Quantitative proteomics identifies a Dab2/integrin module regulating cell migration

Teckchandani, Anjali, Toida, Natalie, Goodchild, Jake, Henderson, Christine, Watts, Julian, Wollscheid, Bernd, Cooper, Jonathan A.·2009·Journal of Cell Biology
DOI 10.1083/jcb.200812160PMC PMC2712992
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Abstract

Clathrin-associated endocytic adapters recruit cargoes to coated pits as a first step in endocytosis. We developed an unbiased quantitative proteomics approach to identify and quantify glycoprotein cargoes for an endocytic adapter, Dab2. Surface levels of integrins β1, α1, α2, and α3 but not α5 or αv chains were specifically increased on Dab2-deficient HeLa cells. Dab2 colocalizes with integrin β1 in coated pits that are dispersed over the cell surface, suggesting that it regulates bulk endocytosis of inactive integrins. Depletion of Dab2 inhibits cell migration and polarized movement of integrin β1 and vinculin to the leading edge. By manipulating intracellular and surface integrin β1 levels, we show that migration speed correlates with the intracellular integrin pool but not the surface level. Together, these results suggest that Dab2 internalizes integrins freely diffusing on the cell surface and that Dab2 regulates migration, perhaps by maintaining an internal pool of integrins that can be recycled to create new adhesions at the leading edge.

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  • Dab2 tumor suppressor function is attributed to cell adhesion/migration.

    “and cell adhesion/migration (Chetrit et al., 2009; Chao and Kunz, 2009; Chetrit et al., 2009; Teckchandani et al., 2009; Xie et al., 2015).”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Teckchandani et al., 2009

    The Results report that removing Dab2 inhibited HeLa cell migration on collagen IV, supporting a role in migration. But the Introduction says it is unclear whether Dab2’s roles in cancer and migration share a mechanism, and the Discussion considers an effect on adhesion unlikely to explain its migration result. The paper therefore does not establish that Dab2’s tumor-suppressor function is attributable to adhesion or migration. (LLM, conf=0.85)

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Metadata

Authors
Teckchandani, A., Toida, N., Goodchild, J., Henderson, C., Watts, J., Wollscheid, B., & Cooper, J. A.
Affiliations
  • Fred Hutchinson Cancer Research Center, Seattle, WA 98109 1
  • Institute for Systems Biology, Seattle, WA 98103 2
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2009-07-06
Volume
186
Issue
1
Pages
99-111
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.200812160
PMC
PMC2712992
Cited by
110
References
3
Language
en

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