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J Biol Chem, Vol. 274, Issue 44, 31553-31558, October 29, 1999

Cloning and Characterization of a Novel Human Phosphatidylinositol Transfer Protein, rdgB

Yvonne Fullwood, Maria dos Santos, and J. Justin Hsuan^¶

From the  Ludwig Institute for Cancer Research, Courtauld Building, 91 Riding House St., London W1P 8BT, United Kingdom and the ^¶ Department of Medicine, Royal Free and University College Medical School, University College London, Royal Free Campus, Rowland Hill St., London NW3 2PF, United Kingdom

The various PITP, retinal degeneration B (rdgB), and amino-terminal domain interacting receptor (Nir) phosphatidylinositol transfer proteins can be divided into two structural families. The small, soluble PITP isoforms contain only a phosphatidylinositol transfer domain and have been implicated in phosphoinositide signaling and vesicle trafficking. In contrast, the rdgB proteins, which include Nir2 and Nir3, contain an amino-terminal PITP-like domain, an acidic, Ca²⁺-binding domain, six putative transmembrane domains, and a conserved carboxyl-terminal domain. However, the biological function of rdgB proteins is unclear. Here, we report the isolation of a cDNA encoding a novel rdgB protein, mammalian rdgB (MrdgB). The 38-kDa MrdgB protein contains an amino-terminal PITP-like domain and a short carboxyl-terminal domain. In contrast to other rdgB-like proteins, MrdgB contains no transmembrane motifs or the conserved carboxyl-terminal domain. Using Northern and reverse transcription-polymerase chain reaction analysis, we demonstrate that MrdgB mRNA is ubiquitously expressed. Immunofluorescence analysis of ectopic MrdgB showed cytoplasmic staining, and the ability of recombinant MrdgB to transfer phosphatidylinositol in vitro was similar to other PITP-like domains. Although early reports found functional degeneracy in vitro, the identification of a fifth mammalian PITP-like protein with a unique domain organization and widespread expression supports more recent results that suggest that different PITP-like domains have distinct functions in vivo.

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