eprintid: 1473392
rev_number: 27
eprint_status: archive
userid: 608
dir: disk0/01/47/33/92
datestamp: 2016-02-22 12:40:55
lastmod: 2021-11-30 00:36:10
status_changed: 2016-02-22 12:40:55
type: article
metadata_visibility: show
creators_name: Cockcroft, S
creators_name: Garner, K
creators_name: Yadav, S
creators_name: Gomez-Espinoza, E
creators_name: Raghu, P
title: RdgBα reciprocally transfers PA and PI at ER-PM contact sites to maintain PI(4,5)P2 homoeostasis during phospholipase C signalling in Drosophila photoreceptors
ispublished: pub
divisions: UCL
divisions: B02
divisions: C08
divisions: D09
divisions: G02
keywords: 5-bisphosphate [PI(4,5)P2], endoplasmic reticulum–plasma membrane (ER—PM) contact sites, phosphatidic acid, phosphatidic acid (PA) transport proteins, phosphatidylinositol, phosphatidylinositol 4, phosphatidylinositol transfer protein (PITP), phospholipase C, phototransduction, retinal degeneration type B (RdgB)
note: © 2016 Authors; published by Portland Press Limited.
abstract: Phosphatidylinositol (PI) is the precursor lipid for the synthesis of PI 4,5-bisphosphate [PI(4,5)P2] at the plasma membrane (PM) and is sequentially phosphorylated by the lipid kinases, PI 4-kinase and phosphatidylinositol 4-phosphate (PI4P)-5-kinase. Receptor-mediated hydrolysis of PI(4,5)P2 takes place at the PM but PI resynthesis occurs at the endoplasmic reticulum (ER). Thus PI(4,5)P2 resynthesis requires the reciprocal transport of two key intermediates, phosphatidic acid (PA) and PI between the ER and the PM. PI transfer proteins (PITPs), defined by the presence of the PITP domain, can facilitate lipid transfer between membranes; the PITP domain comprises a hydrophobic cavity with dual specificity but accommodates a single phospholipid molecule. The class II PITP, retinal degeneration type B (RdgB)α is a multi-domain protein and its PITP domain can bind and transfer PI and PA. In Drosophila photoreceptors, a well-defined G-protein-coupled phospholipase Cβ (PLCβ) signalling pathway, phototransduction defects resulting from loss of RdgBα can be rescued by expression of the PITP domain provided it is competent for both PI and PA transfer. We propose that RdgBα proteins maintain PI(4,5)P2 homoeostasis after PLC activation by facilitating the reciprocal transport of PA and PI at ER-PM membrane contact sites.
date: 2016-02-15
official_url: http://dx.doi.org/10.1042/BST20150228
oa_status: green
full_text_type: other
language: eng
primo: open
primo_central: open_green
article_type_text: Journal Article
verified: verified_manual
elements_id: 1094858
doi: 10.1042/BST20150228
pii: BST20150228
lyricists_name: Cockcroft, Shamshad
lyricists_id: SCOCK81
actors_name: Cockcroft, Shamshad
actors_id: SCOCK81
actors_role: owner
full_text_status: public
publication: Biochemical Society Transactions
volume: 44
number: 1
pagerange: 286-292
event_location: England
issn: 1470-8752
citation:        Cockcroft, S;    Garner, K;    Yadav, S;    Gomez-Espinoza, E;    Raghu, P;      (2016)    RdgBα reciprocally transfers PA and PI at ER-PM contact sites to maintain PI(4,5)P2 homoeostasis during phospholipase C signalling in Drosophila photoreceptors.                   Biochemical Society Transactions , 44  (1)   pp. 286-292.    10.1042/BST20150228 <https://doi.org/10.1042/BST20150228>.       Green open access   
 
document_url: https://discovery.ucl.ac.uk/id/eprint/1473392/1/biochem%20Soc%20trans%202015%20Review%20v13%20with%20Fig.pdf