Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis

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Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis. / Dove, Stephen K.; Cooke, Frank T.; Douglas, Michael R.; Sayers, Lee G.; Parker, Peter J.; Michell, Robert H.

In: Nature, Vol. 390, No. 6656, 13.11.1997, p. 187-192.

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Dove, Stephen K. ; Cooke, Frank T. ; Douglas, Michael R. ; Sayers, Lee G. ; Parker, Peter J. ; Michell, Robert H. / Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis. In: Nature. 1997 ; Vol. 390, No. 6656. pp. 187-192.

Bibtex

@article{40f617e1d7774e6e944c957ee371ac3a,
title = "Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis",
abstract = "Inositol phospholipids play multiple roles in cell signaling systems. Two widespread eukaryotic phosphoinositide-based signal transduction mechanisms, phosphoinositidase C-catalysed phosphatidylinositol-4,5- bisphosphate (PtdIns(4,5)P2) hydrolysis and 3-OH kinase-catalysed PtdIns(4,5)P2 phosphorylation, make the second messengers inositol 1,4,5- trisphosphate (Ins(1,4,5)P3) sn-1,2-diacylglycerol and PtdIns(3,4,5)P3 (refs 1-7). In addition, PtdIns(4,5)P2 and PtdIns3P have been implicated in exocytosis and membrane trafficking. We now show that when the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe are hyperosmotically stressed, they rapidly synthesize phosphatidy-linositol-3,5-bisphosphate (PtdIns(3,5)P2) by a process that involves activation of a PtdIns3P 5-OH kinase. This PtdIns(3,5)P2 accumulation only occurs in yeasts that have an active vps34-encoded PtdIns 3-OH kinase, showing that this latter kinase makes the PtdIns3P needed for PtdIns(3,5)P2 synthesis and indicating that PtdIns(3,5)P2 may have a role in sorting vesicular proteins. PtdIns(3,5)P2 is also present in mammalian and plant cells: in monkey Cos-7 cells, its labelling is inversely related to the external osmotic pressure. The stimulation of a PtdIns3P 5-OH kinase-catalysed synthesis of PtdIns(3,5)P2, a molecule that might be a new type of phosphoinositide second messenger, thus appears to be central to a widespread and previously uncharacterized regulatory pathway.",
author = "Dove, {Stephen K.} and Cooke, {Frank T.} and Douglas, {Michael R.} and Sayers, {Lee G.} and Parker, {Peter J.} and Michell, {Robert H.}",
year = "1997",
month = nov,
day = "13",
doi = "10.1038/36613",
language = "English",
volume = "390",
pages = "187--192",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6656",

}

RIS

TY - JOUR

T1 - Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis

AU - Dove, Stephen K.

AU - Cooke, Frank T.

AU - Douglas, Michael R.

AU - Sayers, Lee G.

AU - Parker, Peter J.

AU - Michell, Robert H.

PY - 1997/11/13

Y1 - 1997/11/13

N2 - Inositol phospholipids play multiple roles in cell signaling systems. Two widespread eukaryotic phosphoinositide-based signal transduction mechanisms, phosphoinositidase C-catalysed phosphatidylinositol-4,5- bisphosphate (PtdIns(4,5)P2) hydrolysis and 3-OH kinase-catalysed PtdIns(4,5)P2 phosphorylation, make the second messengers inositol 1,4,5- trisphosphate (Ins(1,4,5)P3) sn-1,2-diacylglycerol and PtdIns(3,4,5)P3 (refs 1-7). In addition, PtdIns(4,5)P2 and PtdIns3P have been implicated in exocytosis and membrane trafficking. We now show that when the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe are hyperosmotically stressed, they rapidly synthesize phosphatidy-linositol-3,5-bisphosphate (PtdIns(3,5)P2) by a process that involves activation of a PtdIns3P 5-OH kinase. This PtdIns(3,5)P2 accumulation only occurs in yeasts that have an active vps34-encoded PtdIns 3-OH kinase, showing that this latter kinase makes the PtdIns3P needed for PtdIns(3,5)P2 synthesis and indicating that PtdIns(3,5)P2 may have a role in sorting vesicular proteins. PtdIns(3,5)P2 is also present in mammalian and plant cells: in monkey Cos-7 cells, its labelling is inversely related to the external osmotic pressure. The stimulation of a PtdIns3P 5-OH kinase-catalysed synthesis of PtdIns(3,5)P2, a molecule that might be a new type of phosphoinositide second messenger, thus appears to be central to a widespread and previously uncharacterized regulatory pathway.

AB - Inositol phospholipids play multiple roles in cell signaling systems. Two widespread eukaryotic phosphoinositide-based signal transduction mechanisms, phosphoinositidase C-catalysed phosphatidylinositol-4,5- bisphosphate (PtdIns(4,5)P2) hydrolysis and 3-OH kinase-catalysed PtdIns(4,5)P2 phosphorylation, make the second messengers inositol 1,4,5- trisphosphate (Ins(1,4,5)P3) sn-1,2-diacylglycerol and PtdIns(3,4,5)P3 (refs 1-7). In addition, PtdIns(4,5)P2 and PtdIns3P have been implicated in exocytosis and membrane trafficking. We now show that when the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe are hyperosmotically stressed, they rapidly synthesize phosphatidy-linositol-3,5-bisphosphate (PtdIns(3,5)P2) by a process that involves activation of a PtdIns3P 5-OH kinase. This PtdIns(3,5)P2 accumulation only occurs in yeasts that have an active vps34-encoded PtdIns 3-OH kinase, showing that this latter kinase makes the PtdIns3P needed for PtdIns(3,5)P2 synthesis and indicating that PtdIns(3,5)P2 may have a role in sorting vesicular proteins. PtdIns(3,5)P2 is also present in mammalian and plant cells: in monkey Cos-7 cells, its labelling is inversely related to the external osmotic pressure. The stimulation of a PtdIns3P 5-OH kinase-catalysed synthesis of PtdIns(3,5)P2, a molecule that might be a new type of phosphoinositide second messenger, thus appears to be central to a widespread and previously uncharacterized regulatory pathway.

UR - http://www.scopus.com/inward/record.url?scp=0030669546&partnerID=8YFLogxK

U2 - 10.1038/36613

DO - 10.1038/36613

M3 - Article

C2 - 9367158

AN - SCOPUS:0030669546

VL - 390

SP - 187

EP - 192

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6656

ER -