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Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling

Phosphoinositides are essential lipid regulators of trafficking and signaling pathways of all eukaryotic cells. Phosphatidylinositol 4-phosphate (PtdIns4 P ) is an intermediate in the synthesis of several important phosphoinositide species but also serves as a regulatory molecule in its own right. P... Full description

Journal Title: Proceedings of the National Academy of Sciences 04 May 2010, Vol.107(18), p.8225
Main Author: Zsofia Szentpetery
Other Authors: Peter Várnai , Tamas Balla
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1000157107
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recordid: pnas_s107_18_8225
title: Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling
format: Article
creator:
  • Zsofia Szentpetery
  • Peter Várnai
  • Tamas Balla
subjects:
  • Sciences (General)
ispartof: Proceedings of the National Academy of Sciences, 04 May 2010, Vol.107(18), p.8225
description: Phosphoinositides are essential lipid regulators of trafficking and signaling pathways of all eukaryotic cells. Phosphatidylinositol 4-phosphate (PtdIns4 P ) is an intermediate in the synthesis of several important phosphoinositide species but also serves as a regulatory molecule in its own right. Phosphatidylinositol 4-kinases are most abundant in the Golgi but are also found in the plasma membrane and in endocytic compartments. To investigate the role of Golgi PtdIns4 P in orchestrating trafficking events, we used a unique drug-inducible molecular approach to rapidly deplete PtdIns4 P from Golgi membranes by a recruitable Sac1 phosphatase enzyme. The utility of the system was shown by the rapid loss of Golgi localization of PH domains known to bind PtdIns4 P after Sac1 recruitment to the Golgi. Acute PtdIns4 P depletion prevented the exit of cargo from the Golgi destined to both the plasma membrane and the late endosomes and led to the loss of some but not all clathrin adaptors from the Golgi membrane. Rapid PtdIns4 P depletion in the Golgi also impaired but did not eliminate the replenishment of the plasma membrane PtdIns(4,5) P 2 during phospholipase C activation revealing a hitherto unrecognized contribution of Golgi PtdIns4 P to this process. This unique approach will allow further studies on the role of phosphoinositides in endocytic compartments that have evaded detection using the conventional long-term manipulations of inositide kinase and phosphatase activities.
language: eng
source:
identifier: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1000157107
fulltext: fulltext_linktorsrc
issn:
  • 0027-8424
  • 00278424
  • 1091-6490
  • 10916490
url: Link


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titleAcute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling
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descriptionPhosphoinositides are essential lipid regulators of trafficking and signaling pathways of all eukaryotic cells. Phosphatidylinositol 4-phosphate (PtdIns4 P ) is an intermediate in the synthesis of several important phosphoinositide species but also serves as a regulatory molecule in its own right. Phosphatidylinositol 4-kinases are most abundant in the Golgi but are also found in the plasma membrane and in endocytic compartments. To investigate the role of Golgi PtdIns4 P in orchestrating trafficking events, we used a unique drug-inducible molecular approach to rapidly deplete PtdIns4 P from Golgi membranes by a recruitable Sac1 phosphatase enzyme. The utility of the system was shown by the rapid loss of Golgi localization of PH domains known to bind PtdIns4 P after Sac1 recruitment to the Golgi. Acute PtdIns4 P depletion prevented the exit of cargo from the Golgi destined to both the plasma membrane and the late endosomes and led to the loss of some but not all clathrin adaptors from the Golgi membrane. Rapid PtdIns4 P depletion in the Golgi also impaired but did not eliminate the replenishment of the plasma membrane PtdIns(4,5) P 2 during phospholipase C activation revealing a hitherto unrecognized contribution of Golgi PtdIns4 P to this process. This unique approach will allow further studies on the role of phosphoinositides in endocytic compartments that have evaded detection using the conventional long-term manipulations of inositide kinase and phosphatase activities.
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Phosphoinositides are essential lipid regulators of trafficking and signaling pathways of all eukaryotic cells. Phosphatidylinositol 4-phosphate (PtdIns4 P ) is an intermediate in the synthesis of several important phosphoinositide species but also serves as a regulatory molecule in its own right. Phosphatidylinositol 4-kinases are most abundant in the Golgi but are also found in the plasma membrane and in endocytic compartments. To investigate the role of Golgi PtdIns4 P in orchestrating trafficking events, we used a unique drug-inducible molecular approach to rapidly deplete PtdIns4 P from Golgi membranes by a recruitable Sac1 phosphatase enzyme. The utility of the system was shown by the rapid loss of Golgi localization of PH domains known to bind PtdIns4 P after Sac1 recruitment to the Golgi. Acute PtdIns4 P depletion prevented the exit of cargo from the Golgi destined to both the plasma membrane and the late endosomes and led to the loss of some but not all clathrin adaptors from the Golgi membrane. Rapid PtdIns4 P depletion in the Golgi also impaired but did not eliminate the replenishment of the plasma membrane PtdIns(4,5) P 2 during phospholipase C activation revealing a hitherto unrecognized contribution of Golgi PtdIns4 P to this process. This unique approach will allow further studies on the role of phosphoinositides in endocytic compartments that have evaded detection using the conventional long-term manipulations of inositide kinase and phosphatase activities.

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Phosphoinositides are essential lipid regulators of trafficking and signaling pathways of all eukaryotic cells. Phosphatidylinositol 4-phosphate (PtdIns4 P ) is an intermediate in the synthesis of several important phosphoinositide species but also serves as a regulatory molecule in its own right. Phosphatidylinositol 4-kinases are most abundant in the Golgi but are also found in the plasma membrane and in endocytic compartments. To investigate the role of Golgi PtdIns4 P in orchestrating trafficking events, we used a unique drug-inducible molecular approach to rapidly deplete PtdIns4 P from Golgi membranes by a recruitable Sac1 phosphatase enzyme. The utility of the system was shown by the rapid loss of Golgi localization of PH domains known to bind PtdIns4 P after Sac1 recruitment to the Golgi. Acute PtdIns4 P depletion prevented the exit of cargo from the Golgi destined to both the plasma membrane and the late endosomes and led to the loss of some but not all clathrin adaptors from the Golgi membrane. Rapid PtdIns4 P depletion in the Golgi also impaired but did not eliminate the replenishment of the plasma membrane PtdIns(4,5) P 2 during phospholipase C activation revealing a hitherto unrecognized contribution of Golgi PtdIns4 P to this process. This unique approach will allow further studies on the role of phosphoinositides in endocytic compartments that have evaded detection using the conventional long-term manipulations of inositide kinase and phosphatase activities.

pubNational Acad Sciences
doi10.1073/pnas.1000157107
urlhttp://www.pnas.org/content/107/18/8225.abstract
lad01Proceedings of the National Academy of Sciences
pages8225-8230
date2010-05-04