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Volume 272, Number 4, Issue of January 24, 1997 pp. 2477-2485
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of p150, an Adaptor Protein for the Human Phosphatidylinositol (PtdIns) 3-Kinase
SUBSTRATE PRESENTATION BY PHOSPHATIDYLINOSITOL TRANSFER PROTEIN TO THE p150·PtdIns 3-KINASE COMPLEX

(Received for publication, September 16, 1996, and in revised form, October 24, 1996)

Christina Panaretou , Jan Domin , Shamshad Cockcroft ^¶ and Michael D. Waterfield

From the  Ludwig Institute of Cancer Research, University College London, Riding House Street, London W1P 8BT, the ^¶ Department of Physiology, University College London, University Street, London WC1E 6JJ, and the  Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT, United Kingdom

Genetic and biochemical studies have shown that the phosphatidylinositol (PtdIns) 3-kinase encoded by the yeast VPS34 gene is required for the efficient sorting and delivery of proteins to the vacuole. A human homologue of the yeast VPS34 gene product has recently been characterized as part of a complex with a cellular protein of 150 kDa (Volinia, S., Dhand, R., Vanhaesebroeck, B., MacDougall, L. K., Stein, R., Zvelebil, M. J., Domin, J., Panaretou, C., and Waterfield, M. D. (1995) EMBO J. 14, 3339-3348). Here, cDNA cloning is used to show that the amino acid sequence of this protein, termed p150, is 29.6% identical and 53% similar to the yeast Vps15p protein, an established regulator of Vps34p. Northern blot analysis showed a ubiquitous tissue distribution for p150 similar to that previously observed with PtdIns 3-kinase. Recombinant p150 associated with PtdIns 3-kinase in vitro in a stable manner, resulting in a 2-fold increase in lipid kinase activity. Addition of phosphatidylinositol transfer protein (PI-TP) further stimulated the lipid kinase activity of the p150·PtdIns 3-kinase complex 3-fold. A PtdIns 3-kinase activity could also be co-immunoprecipitated from human cell lysates using anti-PI-TP antisera. This observation demonstrates that an interaction between a PtdIns 3-kinase and PI-TP occurs in vivo, which further implicates lipid transfer proteins in the regulation of PtdIns 3-kinase activity. These results suggest that the Vps15p·Vps34p complex has been conserved from yeast to man and in both species is involved in protein trafficking.

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