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9.A.78.  The Retinal Degeneration B Protein (RdgB) Family

RdgB catalyzes the transfer of phosphatidylinositol (PI) and phosphatidic acid (PA) between membranes (Garner et al. 2012). It may control the phosphatidylinositol concentration in transport vesicles from the subrhabdomeric cisternae (SRC) to the rhabdomere (Vihtelic et al. 1991) and may also function as a calcium transporter (Vihtelic et al. 1991). Eukaryotic proteins containing a phosphatidylinositol transfer (PITP) domain can be divided into two groups, one consisting of small soluble 35-kDa proteins and the other that are membrane- associated and show sequence similarities to the Drosophila retinal degeneration B (rdgB) protein. The rdgB protein consists of four domains, an amino terminal PITP domain, a Ca2+-binding domain, a transmembrane domain and a carboxyl terminal domain that interacts with the protein tyrosine kinase, PYK2. Three mammalian phosphatidylinositol transfer protein membrane-associated genes (PITPNM1, 2 and 3) with homology to Drosophila rdgB have been described and are expressed in the mammalian retina. The rdgB gene plays a critical role in the invertebrate phototransduction pathway, and homologous genes are considered as candidate genes for human eye diseases. Phylogenetic analysis indicates that the human genes arose by gene duplication that occurred very early in animal evolution (Ocaka et al. 2005).


References associated with 9.A.78 family:

Amarilio, R., S. Ramachandran, H. Sabanay, and S. Lev. (2005). Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction. J. Biol. Chem. 280: 5934-5944. 15545272
Fullwood, Y., M. dos Santos, and J.J. Hsuan. (1999). Cloning and characterization of a novel human phosphatidylinositol transfer protein, rdgBbeta. J. Biol. Chem. 274: 31553-31558. 10531358
Garner, K., A.N. Hunt, G. Koster, P. Somerharju, E. Groves, M. Li, P. Raghu, R. Holic, and S. Cockcroft. (2012). Phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1) binds and transfers phosphatidic acid. J. Biol. Chem. 287: 32263-32276. 22822086
Lev, S., J. Hernandez, R. Martinez, A. Chen, G. Plowman, and J. Schlessinger. (1999). Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol. Cell Biol. 19: 2278-2288. 10022914
Litvak, V., N. Dahan, S. Ramachandran, H. Sabanay, and S. Lev. (2005). Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function. Nat. Cell Biol. 7: 225-234. 15723057
Litvak, V., R. Argov, N. Dahan, S. Ramachandran, R. Amarilio, A. Shainskaya, and S. Lev. (2004). Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion. Mol. Cell 14: 319-330. 15125835
Ocaka, L., C. Spalluto, D.I. Wilson, D.M. Hunt, and S. Halford. (2005). Chromosomal localization, genomic organization and evolution of the genes encoding human phosphatidylinositol transfer protein membrane-associated (PITPNM) 1, 2 and 3. Cytogenet Genome Res 108: 293-302. 15627748
Tian, D., V. Litvak, M. Toledo-Rodriguez, S. Carmon, and S. Lev. (2002). Nir2, a novel regulator of cell morphogenesis. Mol. Cell Biol. 22: 2650-2662. 11909959
Vihtelic, T.S., D.R. Hyde, and J.E. O'Tousa. (1991). Isolation and characterization of the Drosophila retinal degeneration B (rdgB) gene. Genetics 127: 761-768. 1903119