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- W2020052689 endingPage "e1000194" @default.
- W2020052689 startingPage "e1000194" @default.
- W2020052689 abstract "The organization of intra-Golgi trafficking and the nature of the transport intermediates involved (e.g., vesicles, tubules, or tubular continuities) remain incompletely understood. It was recently shown that successive cisternae in the Golgi stack are interconnected by membrane tubules that form during the arrival of transport carriers from the endoplasmic reticulum. Here, we examine the mechanisms of generation and the function of these tubules. In principle, tubule formation might depend on several protein- and/or lipid-based mechanisms. Among the latter, we have studied the phospholipase A(2) (PLA(2))-mediated generation of wedge-shaped lysolipids, with the resulting local positive membrane curvature. We show that the arrival of cargo at the Golgi complex induces the recruitment of Group IVA Ca(2+)-dependent, cytosolic PLA(2) (cPLA(2)alpha) onto the Golgi complex itself, and that this cPLA(2)alpha is required for the formation of the traffic-dependent intercisternal tubules and for intra-Golgi transport. In contrast, silencing of cPLA(2)alpha has no inhibitory effects on peri-Golgi vesicles. These findings identify cPLA(2)alpha as the first component of the machinery that is responsible for the formation of intercisternal tubular continuities and support a role for these continuities in transport through the Golgi complex." @default.
- W2020052689 created "2016-06-24" @default.
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- W2020052689 date "2009-09-15" @default.
- W2020052689 modified "2023-10-16" @default.
- W2020052689 title "Group IV Phospholipase A2α Controls the Formation of Inter-Cisternal Continuities Involved in Intra-Golgi Transport" @default.
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- W2020052689 doi "https://doi.org/10.1371/journal.pbio.1000194" @default.
- W2020052689 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2732982" @default.
- W2020052689 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19753100" @default.
- W2020052689 hasPublicationYear "2009" @default.
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