Phosphatidylinositol transfer proteins: Negotiating the regulatory interface between lipid metabolism and lipid signaling in diverse cellular processes

BioFactors ◽  
2011 ◽  
Vol 37 (4) ◽  
pp. 290-308 ◽  
Author(s):  
Ratna Ghosh ◽  
Vytas A. Bankaitis
Keyword(s):  
Lipid Metabolism ◽  
Lipid Signaling ◽  
Cellular Processes ◽  
Phosphatidylinositol Transfer ◽  
Phosphatidylinositol Transfer Proteins

The role of phosphatidylinositol-transfer proteins at membrane contact sites

2016 ◽  
Vol 44 (2) ◽  
pp. 419-424 ◽  
Author(s):  
Michael Selitrennik ◽  
Sima Lev
Keyword(s):  
Underlying Mechanism ◽  
Cellular Processes ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Compartments ◽  
Potential Mode ◽  
Membrane Contact ◽  
Phosphatidylinositol Transfer ◽  
Phosphatidylinositol Transfer Proteins

Phosphatidylinositol-transfer proteins (PITPs) have been initially identified as soluble factors that accelerate the monomeric exchange of either phosphatidylinositol (PI) or phosphatidylcholine (PC) between membrane bilayers in vitro. They are highly conserved in eukaryotes and have been implicated in different cellular processes, including vesicular trafficking, signal transduction, and lipid metabolism. Recent studies suggest that PITPs function at membrane contact sites (MCSs) to facilitate the transport of PI from its synthesis site at the endoplasmic reticulum (ER) to various membrane compartments. In this review, we describe the underlying mechanism of PITPs targeting to MCSs, discuss their cellular roles and potential mode of action.

scholarly journals Phosphatidylinositol transfer proteins and functional specification of lipid signaling pools

2007 ◽  
Vol 47 (1) ◽  
pp. 27-40 ◽  
Author(s):  
Vytas A. Bankaitis ◽  
Patrick Vincent ◽  
Maria Merkulova ◽  
Kim Tyeryar ◽  
Yang Liu
Keyword(s):  
Lipid Signaling ◽  
Functional Specification ◽  
Phosphatidylinositol Transfer ◽  
Phosphatidylinositol Transfer Proteins

Biological functions of phosphatidylinositol transfer proteins

2004 ◽  
Vol 82 (1) ◽  
pp. 254-262 ◽  
Author(s):  
Sheri M Routt ◽  
Vytas A Bankaitis
Keyword(s):  
Lipid Metabolism ◽  
Protein Secretion ◽  
Plant Development ◽  
Membrane Trafficking ◽  
Biological Functions ◽  
Cellular Functions ◽  
Transfer Protein ◽  
Phosphatidylinositol Transfer ◽  
Available Information ◽  
Phosphatidylinositol Transfer Proteins

Phosphatidylinositol/phosphatidylcholine transfer proteins (PITPs) are ubiquitous and highly conserved proteins that are believed to regulate lipid-mediated signaling events. Their ubiquity and conservation notwithstanding, PITPs remain remarkably uninvestigated. Little is known about the coupling of specific PITPs to explicit cellular functions or the mechanisms by which PITPs interface with apppropriate cellular functions. The available information indicates a role for these proteins in regulating the interface between lipid metabolism and membrane trafficking in yeast, signaling in plant development, the trafficking of specialized luminal cargo in mammalian enterocytes, and neurological function in mammals. Herein, we review recent advances in PITP biology and discuss as yet unresolved issues in this field.Key words: phosphatidylinositol transfer protein, secretion, lipid signaling, phosphoinositide.

An essential role for phosphatidylinositol transfer protein in phospholipase C-Mediated inositol lipid signaling

Cell ◽  
1993 ◽  
Vol 74 (5) ◽  
pp. 919-928 ◽  
Author(s):  
Geraint M.H. Thomas ◽  
Emer Cunningham ◽  
Amanda Fensome ◽  
Andrew Ball ◽  
Nicholas F. Totty ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Essential Role ◽  
Lipid Signaling ◽  
Transfer Protein ◽  
Phosphatidylinositol Transfer Protein ◽  
Phosphatidylinositol Transfer

Phosphatidylinositol transfer proteins and protein kinase C make separate but non-interacting contributions to the phosphorylation state necessary for secretory competence in rat mast cells

2001 ◽  
Vol 356 (1) ◽  
pp. 287-296 ◽  
Author(s):  
Jef A. PINXTEREN ◽  
Bastien D. GOMPERTS ◽  
Danise ROGERS ◽  
Scott E. PHILLIPS ◽  
Peter E. R. TATHAM ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Mast Cells ◽  
Protein Kinase ◽  
Aminoglycoside Antibiotic ◽  
Pleckstrin Homology Domain ◽  
Kinase C ◽  
Streptolysin O ◽  
Regulatory Machinery ◽  
Phosphatidylinositol Transfer ◽  
Phosphatidylinositol Transfer Proteins

Mast cells permeabilized by streptolysin O undergo exocytosis when stimulated with Ca2+ and guanosine 5′-[γ-thio]triphosphate but become progressively refractory to this stimulus if it is delayed. This run-down of responsiveness occurs over a period of 20–30min, during which the cells leak soluble and tethered proteins. We show here that withdrawal of ATP during the process of run-down is strongly inhibitory but that as little as 25μM ATP can extend responsiveness significantly; this effect is maximal at 50μM. When phosphatidylinositol transfer proteins (PITPs) are provided to cells at the time of permeabilization, run-down is retarded. We conclude that in the presence of ATP they convey substrates for phosphorylation that are essential for exocytosis and thus interact with the regulatory machinery. Furthermore, we show that PITPα and PITPβ have additive effects in this mechanism, suggesting that they are not functionally redundant. Alternatively, secretion from run-down cells can be inhibited by the aminoglycoside antibiotic neomycin, which is understood to bind to phosphoinositide headgroups, and by a PH (pleckstrin homology) domain polypeptide that binds phosphoinositides. The apparent displacement of neomycin by exogenous PITPs suggests that these proteins screen essential lipids. Secretion from run-down cells is also inhibited by 1-O-hexadecyl-2-O-methyl-rac-glycerol (AMG-C16), an inhibitor of protein kinase C. The lack of synergy between neomycin and AMG-C16 suggests that protein kinase C independently provides a second essential component through protein phosphorylation and that there are two independent phosphorylation pathways necessary for secretion competence.

Functional Analysis of Phosphatidylinositol Transfer Proteins

1996 ◽  
pp. 327-338 ◽  
Author(s):  
Brian G. Kearns ◽  
James G. Alb ◽  
Robert T. Cartee ◽  
Vytas A. Bankaitis
Keyword(s):  
Functional Analysis ◽  
Phosphatidylinositol Transfer ◽  
Phosphatidylinositol Transfer Proteins
Sign in / Sign up

Export Citation Format

Share Document