Mammalian diseases of phosphatidylinositol transfer proteins and their homologs

Inositol and phosphoinositide signaling pathways represent major regulatory systems in eukaryotes. The physiological importance of these pathways is amply demonstrated by the variety of diseases that involve derangements in individual steps in inositide and phosphoinositide production and degradatio...

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Published inClinical lipidology Vol. 5; no. 6; pp. 867 - 897
Main Authors Nile, Aaron H, Bankaitis, Vytas A, Grabon, Aby
Format Journal Article Book Review
LanguageEnglish
Published United States Future Medicine Ltd 01.12.2010
Taylor & Francis
Taylor & Francis Ltd
Subjects
inositol signaling
lipid metabolism
phosphatidylinositol transfer protein
phosphoinositide
vertebrate disease
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Abstract Inositol and phosphoinositide signaling pathways represent major regulatory systems in eukaryotes. The physiological importance of these pathways is amply demonstrated by the variety of diseases that involve derangements in individual steps in inositide and phosphoinositide production and degradation. These diseases include numerous cancers, lipodystrophies and neurological syndromes. Phosphatidylinositol transfer proteins (PITPs) are emerging as fascinating regulators of phosphoinositide metabolism. Recent advances identify PITPs (and PITP-like proteins) to be coincidence detectors, which spatially and temporally coordinate the activities of diverse aspects of the cellular lipid metabolome with phosphoinositide signaling. These insights are providing new ideas regarding mechanisms of inherited mammalian diseases associated with derangements in the activities of PITPs and PITP-like proteins.
AbstractList Inositol and phosphoinositide signaling pathways represent major regulatory systems in eukaryotes. The physiological importance of these pathways is amply demonstrated by the variety of diseases that involve derangements in individual steps in inositide and phosphoinositide production and degradation. These diseases include numerous cancers, lipodystrophies and neurological syndromes. Phosphatidylinositol transfer proteins (PITPs) are emerging as fascinating regulators of phosphoinositide metabolism. Recent advances identify PITPs (and PITP-like proteins) to be coincidence detectors, which spatially and temporally coordinate the activities of diverse aspects of the cellular lipid metabolome with phosphoinositide signaling. These insights are providing new ideas regarding mechanisms of inherited mammalian diseases associated with derangements in the activities of PITPs and PITP-like proteins.
Inositol and phosphoinositide signaling pathways represent major regulatory systems in eukaryotes. The physiological importance of these pathways is amply demonstrated by the variety of diseases that involve derangements in individual steps in inositide and phosphoinositide production and degradation. These diseases include numerous cancers, lipodystrophies and neurological syndromes. Phosphatidylinositol transfer proteins (PITPs) are emerging as fascinating regulators of phosphoinositide metabolism. Recent advances identify PITPs (and PITP-like proteins) to be coincidence detectors, which spatially and temporally coordinate the activities of diverse aspects of the cellular lipid metabolome with phosphoinositide signaling. These insights are providing new ideas regarding mechanisms of inherited mammalian diseases associated with derangements in the activities of PITPs and PITP-like proteins.Inositol and phosphoinositide signaling pathways represent major regulatory systems in eukaryotes. The physiological importance of these pathways is amply demonstrated by the variety of diseases that involve derangements in individual steps in inositide and phosphoinositide production and degradation. These diseases include numerous cancers, lipodystrophies and neurological syndromes. Phosphatidylinositol transfer proteins (PITPs) are emerging as fascinating regulators of phosphoinositide metabolism. Recent advances identify PITPs (and PITP-like proteins) to be coincidence detectors, which spatially and temporally coordinate the activities of diverse aspects of the cellular lipid metabolome with phosphoinositide signaling. These insights are providing new ideas regarding mechanisms of inherited mammalian diseases associated with derangements in the activities of PITPs and PITP-like proteins.
Author Nile, Aaron H
Bankaitis, Vytas A
Grabon, Aby
AuthorAffiliation vytas@med.unc.edu
1Department of Cell & Developmental Biology, Lineberger Comprehensive Cancer Center School of Medicine University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-27090, USA
AuthorAffiliation_xml – name: 1Department of Cell & Developmental Biology, Lineberger Comprehensive Cancer Center School of Medicine University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-27090, USA
– name: vytas@med.unc.edu
– name: 1 Department of Cell & Developmental Biology, Lineberger Comprehensive Cancer Center School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-27090, USA
Author_xml – sequence: 1
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  surname: Nile
  fullname: Nile, Aaron H
– sequence: 2
  givenname: Vytas A
  surname: Bankaitis
  fullname: Bankaitis, Vytas A
– sequence: 3
  givenname: Aby
  surname: Grabon
  fullname: Grabon, Aby
BackLink https://www.ncbi.nlm.nih.gov/pubmed/21603057$$D View this record in MEDLINE/PubMed
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Snippet Inositol and phosphoinositide signaling pathways represent major regulatory systems in eukaryotes. The physiological importance of these pathways is amply...
SourceID pubmedcentral
proquest
pubmed
crossref
informaworld
futurescience
SourceType Open Access Repository
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SubjectTerms inositol signaling
lipid metabolism
phosphatidylinositol transfer protein
phosphoinositide
vertebrate disease
Title Mammalian diseases of phosphatidylinositol transfer proteins and their homologs
URI http://dx.doi.org/10.2217/clp.10.67
https://www.tandfonline.com/doi/abs/10.2217/clp.10.67
https://www.ncbi.nlm.nih.gov/pubmed/21603057
https://www.proquest.com/docview/817139205
https://www.proquest.com/docview/1835414840
https://pubmed.ncbi.nlm.nih.gov/PMC3097519
Volume 5
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