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Originally published as MBC in Press, 10.1091/mbc.E01-10-0096 on April 24, 2002
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Vol. 13, Issue 7, 2374-2382, July 2002

Differential Recognition of Tyrosine-based Basolateral Signals by AP-1B Subunit µ1B in Polarized Epithelial Cells

Hisashi Sugimoto,*dagger Masayuki Sugahara,* Heike Fölsch,Dagger Yasuhiro Koide,*§ Fubito Nakatsu,*§ Naotaka Tanaka,* Toshiro Nishimura,dagger Mitsuru Furukawa,dagger Chris Mullins,|| Nobuhiro Nakamura,* Ira Mellman,Dagger and Hiroshi Ohno*§

 *Division of Molecular Membrane Biology, Cancer Research Institute, and  dagger Department of Otorhinolaryngology, Head and Neck Surgery, Kanazawa University Graduate School of Medical Science, Kanazawa, Ishikawa 920-0934, Japan;  Dagger Department of Cell Biology and Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, Connecticut 06520-8002;  §RIKEN Research Center for Allergy and Immunology, Yokohama, Kanagawa 230-0045, Japan; and  ||Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-5430

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 low-density lipoprotein receptors) accumulate at the basolateral domain normally, although in a manner 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 ways.

Corresponding author. E-mail address: hohno{at}kenroku.kanazawa-u.ac.jp.

Molecular Biology of the Cell
Vol. 13, 2374-2382, July 2002
Copyright © 2002 by The American Society for Cell Biology


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