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Published 22 December 2003. doi:10.1083/jcb.200307157
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© The Rockefeller University Press, 0021-9525/2003/12/1281 $8.00
The Journal of Cell Biology, Volume 163, Number 6, 1281-1290

Article

 Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 {gamma}–{sigma}1 and AP-3 {delta}–{sigma}3 hemicomplexes

Katy Janvier1, Yukio Kato1, Markus Boehm1, Jeremy R. Rose2, José A. Martina1, Bong-Yoon Kim1, Sundararajan Venkatesan2 and Juan S. Bonifacino1

1 Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development
2 Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892

Address correspondence to Juan S. Bonifacino, Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Building 18T, Rm. 101, Bethesda, MD 20892. Tel.: (301) 496-6368. Fax: (301) 402-0078. email: juan{at}helix.nih.gov

The sorting of transmembrane proteins to endosomes and lysosomes is mediated by signals present in the cytosolic tails of the proteins. A subset of these signals conform to the [DE]XXXL[LI] consensus motif and mediate sorting via interactions with heterotetrameric adaptor protein (AP) complexes. However, the identity of the AP subunits that recognize these signals remains controversial. We have used a yeast three-hybrid assay to demonstrate that [DE]XXXL[LI]-type signals from the human immunodeficiency virus negative factor protein and the lysosomal integral membrane protein II interact with combinations of the {gamma} and {sigma}1 subunits of AP-1 and the {delta} and {sigma}3 subunits of AP-3, but not the analogous combinations of AP-2 and AP-4 subunits. The sequence requirements for these interactions are similar to those for binding to the whole AP complexes in vitro and for function of the signals in vivo. These observations reveal a novel mode of recognition of sorting signals involving the {gamma}/{delta} and {sigma} subunits of AP-1 and AP-3.

Key Words: clathrin; adaptors; coats; endocytosis; endosomes

Y. Kato's present address is Faculty of Pharmaceutical Sciences, Kanazawa University, 13-1 Takara-machi, Kanazawa, 920-0934, Japan.

M. Boehm's present address is ALTANA Pharma AG, Byk-Gulden-Strasse 2, 78467 Konstanz, Germany.

Abbreviations used in this paper: 3AT, 3-aminotriazole; AP, adaptor protein; CD-MPR, cation-dependent MPR; CI-MPR, cation-independent MPR; GAL4AD, GAL4, transcription activation domain; GAL4BD, GAL4 DNA binding domain; GGAs, Golgi-localized, {gamma}-ear–containing, Arf-binding proteins; HIV, human immunodeficiency virus; LIMP-II, lysosomal integral membrane protein II; MPR, mannose 6-phosphate receptor; Nef, negative factor; SIV, simian immunodeficiency virus; VHS, Vps27, Hrs, and Stam.


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