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Cited by 222

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Myosin VI Binds to and Localises with Dab2, Potentially Linking Receptor‐Mediated Endocytosis and the Actin Cytoskeleton

Morris, Shelli M., Arden, Susan D., Roberts, Rhys C., Kendrick‐Jones, John, Cooper, Jonathan A., Luzio, J. Paul, Buss, Folma·2002·Traffic
DOI 10.1034/j.1600-0854.2002.30503.x
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Abstract

Myosin VI, an actin‐based motor protein, and Disabled 2 (Dab2), a molecule involved in endocytosis and cell signalling, have been found to bind together using yeast and mammalian two‐hybrid screens. In polarised epithelial cells, myosin VI is known to be associated with apical clathrin‐coated vesicles and is believed to move them towards the minus end of actin filaments, away from the plasma membrane and into the cell. Dab2 belongs to a group of signal transduction proteins that bind in vitro to the FXNPXY sequence found in the cytosolic tails of members of the low‐density lipoprotein receptor family. The central region of Dab2, containing two DPF motifs, binds to the clathrin adaptor protein AP‐2, whereas a C‐terminal region contains the binding site for myosin VI. This site is conserved in Dab1, the neuronal counterpart of Dab2. The interaction between Dab2 and myosin VI was confirmed by in vitro binding assays and coimmunoprecipitation and by their colocalisation in clathrin‐coated pits/vesicles concentrated at the apical domain of polarised cells. These results suggest that the myosin VI–Dab2 interaction may be one link between the actin cytoskeleton and receptors undergoing endocytosis.

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Crossref · 10.1034/j.1600-0854.2002.30503.x

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1 of 1 references verified0 citation errors · 0 not checkable

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  • Dab2 probably plays an important role in targeting myosin VI to clathrin-coated vesicles.

    “Myosin VI is a component of some clathrin-coated vesicles (Buss et al., 2001) and Dab2 probably plays an important role in targeting this motor to the vesicle.”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Morris et al., 2002a

  • The C-terminus of Dab2 binds the myosin VI motor protein.

    “The C-terminus binds to the myosin VI motor protein (Inoue et al., 2002; Morris et al., 2002a; Hasson, 2003; Spudich et al., 2007).”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Morris et al., 2002a

  • Through its PTB domain, Dab2 mediates attachment of cargos containing transmembrane proteins with an NPXY motif, such as LDL receptor, EGF receptor, megalin, and integrins, to clathrin coats.

    “Through its PTB domain, Dab2 mediates the attachment of cargos containing transmembrane proteins with an NPXY motif, such as the LDL receptor, EGF receptor, megalin, and integrins, to clathrin coats”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Morris et al., 2002a

  • Dab2 links clathrin-coated cargos containing transmembrane proteins with an NPXY motif to the myosin motor, facilitating their endocytosis and directional trafficking.

    “Thus, Dab2 links clathrin-coated cargos containing transmembrane proteins with an NPXY motif to the myosin motor, facilitating their endocytosis and directional trafficking”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Morris et al., 2002a

Citations

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Metadata

Authors
Morris, S. M., Arden, S. D., Roberts, R. C., Kendrick‐Jones, J., Cooper, J. A., Luzio, J. P., & Buss, F.
Venue
Traffic
Publisher
Wiley
Published
2002-05
Volume
3
Issue
5
Pages
331-341
ISSN
  • 1398-9219
  • 1600-0854
DOI
10.1034/j.1600-0854.2002.30503.x
Cited by
222
References
1
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 207 d)

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