2009
DOI: 10.1371/journal.pbio.1000194
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Group IV Phospholipase A2α Controls the Formation of Inter-Cisternal Continuities Involved in Intra-Golgi Transport

Abstract: The enzyme phospholipase A2 (cPLA2α) is involved in the formation of intercisternal tubules that mediate transport of proteins within the Golgi complex.

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Cited by 84 publications
(133 citation statements)
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“…In addition, in the IMLF Ϫ/Ϫ cells from the PLA 2 IV␣ knock-out mice, the PLA 2 IV␣ N-terminal C2 domain was identified as the portion of PLA 2 IV␣ that is sufficient to induce a rescue of impaired FcR-mediated phagocytosis. This is in agreement with previous studies, also from our laboratory, that have indicated the C2 domain as the minimal PLA 2 IV␣ portion that can still translocate to cell membranes following increases in intracellular Ca 2ϩ (18). Based on the data presented here, we speculate on a new mechanism of action of PLA 2 IV␣, whereby membrane insertion of the PLA 2 IV␣ C2 domain induces perturbation of the membrane phospholipid packing, potentially also generating the membrane bending that is necessary for phagosome formation (57).…”
Section: Discussionsupporting
confidence: 94%
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“…In addition, in the IMLF Ϫ/Ϫ cells from the PLA 2 IV␣ knock-out mice, the PLA 2 IV␣ N-terminal C2 domain was identified as the portion of PLA 2 IV␣ that is sufficient to induce a rescue of impaired FcR-mediated phagocytosis. This is in agreement with previous studies, also from our laboratory, that have indicated the C2 domain as the minimal PLA 2 IV␣ portion that can still translocate to cell membranes following increases in intracellular Ca 2ϩ (18). Based on the data presented here, we speculate on a new mechanism of action of PLA 2 IV␣, whereby membrane insertion of the PLA 2 IV␣ C2 domain induces perturbation of the membrane phospholipid packing, potentially also generating the membrane bending that is necessary for phagosome formation (57).…”
Section: Discussionsupporting
confidence: 94%
“…Here, both phagocytosis-induced release of arachidonic acid and FcR-mediated phagocytosis were monitored. The PLA 2 IV␣ enzymatic activity was completely inhibited by this treatment (Table 1), whereas FcR-mediated phago- (1-525), and the point mutant GFP-PLA 2 IV␣-S228C have no catalytic activity, but they translocate to membranes under agonist stimulation (18,36,55). The point mutant GFP-PLA 2 IV␣-D43N cannot translocate to membranes under cell stimulation (12).…”
Section: Fcr-mediated Phagocytosis Selectively Stimulates Pla 2 Iv␣-mmentioning
confidence: 94%
“…The intracellular localization of GDE4 was further examined by comparing the staining patterns in COS-7 cells with PLA 2 IV␣, which under these conditions showed a diffuse localization (cytosolic) as well as a perinuclear staining compatible with a Golgi localization (Fig. 3B), in agreement with the reported localization of this enzyme (25). The results showed that heterologous GDE4 partially co-localized with overexpressed PLA 2 IV␣, suggesting its prevalent Golgi localization (Fig.…”
Section: Isolation Of Two Novel Members Of the Glycerophosphodiestersupporting
confidence: 83%
“…It is important to note that two stacks are not needed to accomplish such transport: because even ministack cisternae are discontinuous, such a fusion event could occur between cisternae within a ministack. In addition, this class of fusion may explain the tubules that have been detected in some laboratories to connect Golgi cisternae (4,5,30).…”
Section: Combining Premises 1 Andmentioning
confidence: 94%