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AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells

Simmen, Thomas, Höning, Stefan, Icking, Ann, Tikkanen, Ritva, Hunziker, Walter·2002·Nature Cell Biology

Abstract

Adaptors are heterotetrameric complexes that mediate the incorporation of cargo into transport vesicles by interacting with sorting signals present in the cytosolic domain of transmembrane proteins. Four adaptors, AP-1 (beta 1, gamma, mu 1A or mu 1B, sigma 1), AP-2 (beta 2, alpha, mu 2, sigma 2), AP-3 (beta 3 , delta, mu 3, sigma 3) or AP-4 (beta 4, epsilon, mu 4, sigma 4), have been characterized. AP-1 and AP-3 mediate sorting events at the level of the TGN and/or endosomes, whereas AP-2 functions in endocytic clathrin coated vesicle formation; no function is known so far for AP-4. Here, we show that AP-4 can bind different types of cytosolic signals known to mediate basolateral transport in epithelial cells. Furthermore, in MDCK cells with depleted mu 4 protein levels, several basolateral proteins are mis-sorted to the apical surface, showing that AP-4 participates in basolateral sorting in epithelial cells.

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Crossref · 10.1038/ncb745

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  • The proteins involved in decoding basolateral sorting signals have been the widely expressed AP4 complex and the clathrin adaptor complex AP1B, both acting predominantly upon Y-dependent motifs.

    “So far, the proteins involved in decoding basolateral sorting signals have been the widely expressed AP4 complex (Simmen et al., 2002) and the clathrin adaptor complexes AP1B complex specifically expressed by certain epithelial cells (Folsch et al., 1999; Ohno et al., 1999; Gan et al., 2002), both acting predominantly upon Y-dependent motifs.”

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Metadata

Authors
Simmen, T., Höning, S., Icking, A., Tikkanen, R., & Hunziker, W.
Venue
Nature Cell Biology
Published
2002-01-21
Volume
4
Issue
2
Pages
154-159
ISSN
  • 1465-7392
  • 1476-4679
Cited by
189
References
0
Language
en

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