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Assembly of Clathrin Coats Disrupts the Association between Eps15 and AP-2 Adaptors

Cupers, Philippe, Jadhav, Ashutosh P., Kirchhausen, Tomas·1998·Journal of Biological Chemistry
DOI 10.1074/jbc.273.4.1847
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Abstract

Eps15 is a phosphorylation substrate of the epidermal growth factor receptor kinase. In vivo, it is largely found in complex with AP-2, the plasma membrane clathrin adaptor protein complex. Although AP-2 is uniformly distributed across the surface of clathrin-coated pits and vesicles, Eps15 is preferentially found in the rims of endocytic clathrin-coated pits (1). This observation suggests that Eps15 may disengage from AP-2 during coat formation. Here we use two new anti-Eps15 antibodies to show that, contrary to our own earlier suggestion, coated vesicles isolated from brain do not contain detectable amounts of Eps15. Furthermore, when AP-2 complexes that are saturated with Eps15 are used for in vitro assembly of clathrin-AP-2 coats, normal structures are formed that contain the expected amounts of clathrin and AP-2, but the amount of Eps15 present is dramatically lower than that of AP-2. We propose that during coated pit formation, addition of clathrin to the growing edge at the rim of the pit releases Eps15 from AP-2.

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  • Extensive clathrin recruitment does not disrupt the interaction between AP-2 and either Dab2 or epsin, AP180 or HIP1.

    “Importantly, and in contrast to eps15 (Cupers et al., 1998), extensive clathrin recruitment does not disrupt the interaction between AP-2 and either Dab2 or epsin (Figure 8) (Mishra et al., 2001), AP180 (Ford et al., 2001) or HIP1 (Mishra et al., 2001), such that these proteins are now released from the membrane surface.”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Cupers et al., 1998

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Research works printed but not linked: 22

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Metadata

Authors
Cupers, P., Jadhav, A. P., & Kirchhausen, T.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-01
Volume
273
Issue
4
Pages
1847-1850
ISSN
0021-9258
DOI
10.1074/jbc.273.4.1847
Cited by
46
References
0
Language
en
Licence

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