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A more recent version of this article appeared on July 1, 2002
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Submitted on October 22, 2001
Revised on February 11, 2002
Accepted on April 5, 2002
1 Division of Molecular Membrane Biology, Cancer Research Institute, Kanazawa University; and Department of Otorhinolaryngology, Head and Neck Surgery, Kanazawa University Graduate School of Medical Science, 13-1 Takaramachi, Kanazawa 920-0934, Japan
2 Division of Molecular Membrane Biology, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920-0934, Japan
3 Department of Cell Biology and Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, Connecticut 06520-8002, USA
4 RIKEN Research Center for Allergy and Immunology, 1-7-22 Suehirocho, Tsurumicu, Yokohama, Kanagawa 230-0045, Japan; and Division of Molecular Membrane Biology, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920-0934, Japan
5 Department of Otorhinolaryngology, Head and Neck Surgery, Kanazawa University Graduate School of Medical Science, 13-1 Takaramachi, Kanazawa 920-0934, Japan
6 Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, 18 Library Drive, Bethesda Maryland 20892-5430, USA
7 Division of Molecular Membrane Biology, Cancer Research Institute, Kanazawa University,13-1 Takaramachi, Kanazawa 920-0934, Japan
8 Division of Molecular Membrane Biology, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920-0934, Japan; and RIKEN Research Center for Allergy and Immunology, 1-7-22 Suehirocho, Tsurumicu, Yokohama, Kanagawa 230-0045, Japan
* Corresponding author. E-mail address: hohno{at}kenroku.kanazawa-u.ac.jp.
To investigate the importance of tyrosine-recognition by the AP-1B clathrin adaptor subunit µ1B for basolateral sorting of integral membrane proteins in polarized epithelial cells, we have produced and characterized a mutant form of µ1B. The mutant (M-µ1B) contains alanine substitutions of each of the four conserved residues which in the AP-2 adaptor subunit µ2 are critical for interacting with tyrosine-based endocytosis signals. We show M-µ1B is defective for tyrosine binding in vitro, but is nevertheless incorporated into AP-1 complexes in transfected cells. Using LLC-PK1 cells expressing either wild type or M-µ1B, we find that there is inefficient basolateral expression of membrane proteins whose basolateral targeting signals share critical tyrosines with signals for endocytosis. In contrast, membrane proteins whose basolateral targeting signals are distinct from their endocytosis signals (transferrin and LDL receptors) accumulate at the basolateral domain normally; although in a fashion that is strictly dependent on µ1B or M-µ1B expression. Our results suggest that µ1B interacts with different classes of basolateral targeting signals in distinct fashions.
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