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A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi.

Polyphosphoinositides are an important class of lipid that recruit specific effector proteins to organelle membranes. One member, phosphatidylinositol 4-phosphate (Ptdlns4P) has been localized to Golgi membranes based on the distribution of lipid binding modules from Ptdlns4P effector proteins. Howe... Full description

Journal Title: The Journal of cell biology April 14, 2014, Vol.205(1), pp.113-126
Main Author: Hammond, Gerald R V
Other Authors: Machner, Matthias P , Balla, Tamas
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1540-8140 ; DOI: 10.1083/jcb.201312072
Link: http://search.proquest.com/docview/1516724194/?pq-origsite=primo
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title: A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi.
format: Article
creator:
  • Hammond, Gerald R V
  • Machner, Matthias P
  • Balla, Tamas
subjects:
  • Animals–Genetics
  • Bacterial Proteins–Metabolism
  • Binding Sites–Metabolism
  • Biosensing Techniques–Metabolism
  • Cos Cells–Metabolism
  • Cell Membrane–Genetics
  • Cercopithecus Aethiops–Metabolism
  • Dogs–Genetics
  • Endosomes–Metabolism
  • Genes, Reporter–Metabolism
  • Golgi Apparatus–Metabolism
  • Guanine Nucleotide Exchange Factors–Metabolism
  • Luminescent Proteins–Metabolism
  • Lysosomes–Metabolism
  • Mice–Metabolism
  • Microscopy, Confocal–Metabolism
  • Minor Histocompatibility Antigens–Metabolism
  • Phosphatidylinositol Phosphates–Metabolism
  • Phosphotransferases (Alcohol Group Acceptor)–Metabolism
  • Protein Structure, Tertiary–Metabolism
  • Recombinant Fusion Proteins–Metabolism
  • Second Messenger Systems–Metabolism
  • Time Factors–Metabolism
  • Time-Lapse Imaging–Metabolism
  • Transfection–Metabolism
  • Rab Gtp-Binding Proteins–Metabolism
  • Bacterial Proteins
  • Guanine Nucleotide Exchange Factors
  • Luminescent Proteins
  • Minor Histocompatibility Antigens
  • Phosphatidylinositol Phosphates
  • Recombinant Fusion Proteins
  • Sidm Protein, Legionella Pneumophila
  • Phosphatidylinositol 4-Phosphate
  • Rab7 Protein
  • Phosphotransferases (Alcohol Group Acceptor)
  • Phosphatidylinositol Phosphate 4-Kinase
  • Rab Gtp-Binding Proteins
ispartof: The Journal of cell biology, April 14, 2014, Vol.205(1), pp.113-126
description: Polyphosphoinositides are an important class of lipid that recruit specific effector proteins to organelle membranes. One member, phosphatidylinositol 4-phosphate (Ptdlns4P) has been localized to Golgi membranes based on the distribution of lipid binding modules from Ptdlns4P effector proteins. However, these probes may be biased by additional interactions with other Golgi-specific determinants. In this paper, we derive a new Ptdlns4P biosensor using the Ptdlns4P binding of SidM (P4M) domain of the secreted effector protein SidM from the bacterial pathogen Legionella pneumophila. Ptdlns4P was necessary and sufficient for localization of P4M, which revealed pools of the lipid associated not only with the Golgi but also with the plasma membrane and Rab7-positive late endosomes/lysosomes. Ptdlns4P distribution was determined by the localization and activities of both its anabolic and catabolic enzymes. Therefore, P4M reports a wider cellular distribution of Ptdlns4P than previous probes and therefore will be valuable for dissecting the biological functions of Ptdlns4Pin its assorted membrane compartments. www.jcb.org/cgi/doi/10.1083/jcb.201312072
language: eng
source:
identifier: E-ISSN: 1540-8140 ; DOI: 10.1083/jcb.201312072
fulltext: fulltext
issn:
  • 15408140
  • 1540-8140
url: Link


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titleA novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi.
creatorHammond, Gerald R V ; Machner, Matthias P ; Balla, Tamas
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identifierE-ISSN: 1540-8140 ; DOI: 10.1083/jcb.201312072
subjectAnimals–Genetics ; Bacterial Proteins–Metabolism ; Binding Sites–Metabolism ; Biosensing Techniques–Metabolism ; Cos Cells–Metabolism ; Cell Membrane–Genetics ; Cercopithecus Aethiops–Metabolism ; Dogs–Genetics ; Endosomes–Metabolism ; Genes, Reporter–Metabolism ; Golgi Apparatus–Metabolism ; Guanine Nucleotide Exchange Factors–Metabolism ; Luminescent Proteins–Metabolism ; Lysosomes–Metabolism ; Mice–Metabolism ; Microscopy, Confocal–Metabolism ; Minor Histocompatibility Antigens–Metabolism ; Phosphatidylinositol Phosphates–Metabolism ; Phosphotransferases (Alcohol Group Acceptor)–Metabolism ; Protein Structure, Tertiary–Metabolism ; Recombinant Fusion Proteins–Metabolism ; Second Messenger Systems–Metabolism ; Time Factors–Metabolism ; Time-Lapse Imaging–Metabolism ; Transfection–Metabolism ; Rab Gtp-Binding Proteins–Metabolism ; Bacterial Proteins ; Guanine Nucleotide Exchange Factors ; Luminescent Proteins ; Minor Histocompatibility Antigens ; Phosphatidylinositol Phosphates ; Recombinant Fusion Proteins ; Sidm Protein, Legionella Pneumophila ; Phosphatidylinositol 4-Phosphate ; Rab7 Protein ; Phosphotransferases (Alcohol Group Acceptor) ; Phosphatidylinositol Phosphate 4-Kinase ; Rab Gtp-Binding Proteins
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descriptionPolyphosphoinositides are an important class of lipid that recruit specific effector proteins to organelle membranes. One member, phosphatidylinositol 4-phosphate (Ptdlns4P) has been localized to Golgi membranes based on the distribution of lipid binding modules from Ptdlns4P effector proteins. However, these probes may be biased by additional interactions with other Golgi-specific determinants. In this paper, we derive a new Ptdlns4P biosensor using the Ptdlns4P binding of SidM (P4M) domain of the secreted effector protein SidM from the bacterial pathogen Legionella pneumophila. Ptdlns4P was necessary and sufficient for localization of P4M, which revealed pools of the lipid associated not only with the Golgi but also with the plasma membrane and Rab7-positive late endosomes/lysosomes. Ptdlns4P distribution was determined by the localization and activities of both its anabolic and catabolic enzymes. Therefore, P4M reports a wider cellular distribution of Ptdlns4P than previous probes and therefore will be valuable for dissecting the biological functions of Ptdlns4Pin its assorted membrane compartments. www.jcb.org/cgi/doi/10.1083/jcb.201312072
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