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Dab2 regulates clathrin assembly and cell spreading

Chetrit, David, Ziv, Naomi, Ehrlich, Marcelo·2009·Biochemical Journal
DOI 10.1042/bj20081288
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Abstract

The recruitment of clathrin to the membrane and its assembly into coated pits results from its interaction with endocytic adaptors and other regulatory proteins in the context of a specific lipid microenvironment. Dab2 (disabled 2) is a mitotic phosphoprotein and a monomeric adaptor for clathrin-mediated endocytosis. In the present study, we employed GFP (green fluorescent protein) fusion constructs of different isoforms and mutants of rat Dab2 and characterized their effect on the size, distribution and dynamics of clathrin assemblies. Enhanced levels of expression of the p82 isoform of Dab2 in COS7 cells induced enlarged clathrin assemblies at the plasma membrane. p82–clathrin assemblies, which concentrate additional endocytic proteins, such as AP2 (adaptor protein 2) and epsin, are dynamic structures in which both p82 and clathrin exchange actively between the membrane-bound and cytosolic sub-populations. The ability of p82 to induce enlarged clathrin assemblies is dependent on the presence of a functional PTB domain (phosphotyrosine-binding domain), on binding to clathrin and phospholipids, and on a newly identified and evolutionarily conserved poly-lysine stretch which precedes the PTB domain. These same molecular features are required for Dab2 to enhance the spreading of COS7 cells on fibronectin. The ability of the p82 isoform of Dab2 to enhance cell spreading was confirmed in both HeLa cells and HBL cells (human breast epithelial cells). COS7 cells expressing GFP–p82 and plated on to fibronectin concentrate the β1 integrin into clathrin–p82 assemblies. Furthermore, during cell spreading, p82–clathrin assemblies concentrate at the site of the initial cell–matrix contact and are absent from regions of intense membrane ruffling. We propose a role for Dab2 and clathrin in integrin-mediated cell spreading.

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  • Studies in cultured cells suggested a role of Dab2 in endocytic recycling and trafficking of integrins and thus impact cell mobility.

    “Studies in cultured cells suggested a role of Dab2 in endocytic recycling and trafficking of integrins and thus impact cell mobility”

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

  • 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 Chetrit et al., 2009

  • Similar GCCSs have been observed in other cell types upon Dab-2 overexpression, associated with integrins, another Dab2-specific cargo molecule.

    “Similar GCCSs have been observed in other cell types upon Dab-2 overexpression, associated with integrins, another Dab2-specific cargo molecule (Chetrit et al., 2009).”

    From Cargo- and adaptor-specific mechanisms regulate clathrin-mediated endocytosis (2010) · cites this paper as Chetrit et al., 2009

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Metadata

Authors
Chetrit, D., Ziv, N., & Ehrlich, M.
Affiliations
Department of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2009-02-25
Volume
418
Issue
3
Pages
701-715
ISSN
  • 0264-6021
  • 1470-8728
DOI
10.1042/bj20081288
Cited by
47
References
5
Language
en

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