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Published online
doi:10.1083/jcb.200608126
The Journal of Cell Biology, Vol. 177, No. 1, 103-114
The Rockefeller University Press, 0021-9525 $30.00
© Au et al.
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Article

Myosin VI is required for sorting of AP-1B–dependent cargo to the basolateral domain in polarized MDCK cells



Josephine Sui-Yan Au1, Claudia Puri2, Gudrun Ihrke2, John Kendrick-Jones1, and Folma Buss2

1 Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
2 Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, England, UK

Correspondence to F. Buss: fb1{at}mole.bio.cam.ac.uk

In polarized epithelial cells, newly synthesized membrane proteins are delivered on specific pathways to either the apical or basolateral domains, depending on the sorting motifs present in these proteins. Because myosin VI has been shown to facilitate secretory traffic in nonpolarized cells, we investigated its role in biosynthetic trafficking pathways in polarized MDCK cells. We observed that a specific splice isoform of myosin VI with no insert in the tail domain is required for the polarized transport of tyrosine motif containing basolateral membrane proteins. Sorting of other basolateral or apical cargo, however, does not involve myosin VI. Site-directed mutagenesis indicates that a functional complex consisting of myosin VI, optineurin, and probably the GTPase Rab8 plays a role in the basolateral delivery of membrane proteins, whose sorting is mediated by the clathrin adaptor protein complex (AP) AP-1B. Our results suggest that myosin VI is a crucial component in the AP-1B–dependent biosynthetic sorting pathway to the basolateral surface in polarized epithelial cells.

J. Au's present address is Cancer Research UK, Cambridge Research Institute, Li Ka-Shing Centre, Cambridge CB2 0RE, England, UK.

G. Ihrke's present address is Dept. of Pharmacology, Uniformed Services University of the Health Sciences, F. Edward Hébert School of Medicine, Bethesda, MD 20814.

Abbreviations used in this paper: AP, adaptor protein complex; CIMR, Cambridge Institute for Medical Research; Fc{gamma}RIIB, Fc {gamma} receptor isoform BII; LDLR, low-density lipoprotein receptor; LI, large insert; NI, no insert; SI, small insert; TfR, transferrin receptor; VSV-G, vesicular stomatitis virus glycoprotein.


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