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Involvement of PITPnm, a Mammalian Homologue of Drosophila rdgB, in Phosphoinositide Synthesis on Golgi Membranes
Phosphatidylinositol transfer protein (PITP) is involved in phospholipase C-mediated signaling and membrane trafficking. We previously reported cloning and characterization of a gene encoding for membrane-bound PITP, named PITPnm , that is a mammalian homologue of the Drosophila retinal degeneration...
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Published in: | The Journal of biological chemistry 1999-07, Vol.274 (29), p.20569-20577 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Phosphatidylinositol transfer protein (PITP) is involved in phospholipase C-mediated signaling and membrane trafficking. We
previously reported cloning and characterization of a gene encoding for membrane-bound PITP, named PITPnm , that is a mammalian homologue of the Drosophila retinal degeneration B (rdgB) gene (Aikawa, Y., Hara, H., and Watanabe, T. (1997) Biochem. Biophys. Res. Commun. 236, 559â564). Here we report the subcellular localization of PITPnm protein and provide evidence for its involvement in
phosphatidylinositol 4-phosphate (PtdIns 4-P) synthesis. PITPnm is an integral membrane protein that largely localized in
close association with membranes of Golgi vacuoles and the endoplasmic reticulum (ER). The amino terminus region of PITPnm
was exposed to cytoplasmic side. Interaction with various phosphoinositides was observed in the amino terminus region spanning
from 196 amino acids to 257 amino acids of PITPnm. At the amino terminus regions of 1â372 amino acids, PITPnm formed a complex
with type III PtdIns 4-kinase. The transmembrane and carboxyl-terminal portions (residues 418â1242) functioned to retain the
PITPnm in the Golgi vacuole. These results suggest that PITPnm plays a role in phosphoinositide synthesis on the Golgi vacuoles
and possibly in the PtdIns signaling pathway in mammalian cells. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.274.29.20569 |