How is the acyl chain composition of phosphoinositides created and does it matter?
lipid metabolism
lipid-binding domains
membranes
phosphatidylinositol
polyunsaturated fatty acids
signalling
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
31 10 2019
31 10 2019
Historique:
received:
06
08
2019
revised:
27
09
2019
accepted:
01
10
2019
pubmed:
28
10
2019
medline:
27
2
2020
entrez:
29
10
2019
Statut:
ppublish
Résumé
The phosphoinositide (PIPn) family of signalling phospholipids are central regulators in membrane cell biology. Their varied functions are based on the phosphorylation pattern of their inositol ring, which can be recognized by selective binding domains in their effector proteins and be modified by a series of specific PIPn kinases and phosphatases, which control their interconversion in a spatial and temporal manner. Yet, a unique feature of PIPns remains largely unexplored: their unusually uniform acyl chain composition. Indeed, while most phospholipids present a range of molecular species comprising acyl chains of diverse length and saturation, PIPns in several organisms and tissues show the predominance of a single hydrophobic backbone, which in mammals is composed of arachidonoyl and stearoyl chains. Despite evolution having favoured this specific PIPn configuration, little is known regarding the mechanisms and functions behind it. In this review, we explore the metabolic pathways that could control the acyl chain composition of PIPns as well as the potential roles of this selective enrichment. While our understanding of this phenomenon has been constrained largely by the technical limitations in the methods traditionally employed in the PIPn field, we believe that the latest developments in PIPn analysis should shed light onto this old question.
Identifiants
pubmed: 31657437
pii: 220942
doi: 10.1042/BST20190205
pmc: PMC6824679
doi:
Substances chimiques
Phosphatidylinositols
0
1-Phosphatidylinositol 4-Kinase
EC 2.7.1.67
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
1291-1305Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BBS/E/B/000C0415
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/P013384/1
Pays : United Kingdom
Informations de copyright
© 2019 The Author(s).
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