| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1950039 | Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids | 2007 | 8 Pages |
The RdgBs are a group of evolutionarily conserved molecules that contain a phosphatidylinositol transfer protein (PITP) domain. However in contrast to classical PITPs (PITPα) with whom they share the conserved PITP domain, these proteins also contain several additional sequence elements whose functional significance remains unknown. The founding member of the family DrdgBα (Drosophila rdgB) appears to be essential for sensory transduction and maintenance of ultra structure in photoreceptors (retinal sensory neurons). Although proposed to support the maintenance of phosphatidylinositol 4, 5 bisphosphate [PI (4, 5) P2] levels during G-protein coupled phospholipase C activity in these cells, the biochemical mechanism of DrdgBα function remains unresolved. More recently, a mammalian RdgB protein has been implicated in the maintenance of diacylglycerol (DAG) levels and secretory function at Golgi membranes. In this review we discuss existing work on the function of RdgB proteins and set out future challenges in understanding this group of lipid transfer proteins.
