Literature DB >> 20874826

A role for phospholipase A2 activity in membrane tubule formation and TGN trafficking.

John A Schmidt1, Danielle N Kalkofen, Kirk W Donovan, William J Brown.   

Abstract

We have investigated the role of phospholipase A(2) (PLA(2) ) enzymes in generating membrane tubules at the trans-Golgi network (TGN). Constitutive TGN membrane tubules and those induced by over-expressing kinase dead protein kinase D were inhibited by the PLA(2) inhibitors ONO-RS-082 (ONO) and bromoenol lactone. These antagonists also inhibited secretory delivery of both soluble and transmembrane cargoes. Finally, use of the reversible antagonist ONO and time-lapse imaging revealed for the first time that PLA(2) antagonists inhibit the initiation of membrane tubule formation at the TGN. Thus, PLA(2) enzymes appear to have an important role in the earliest steps of membrane tubule formation at the TGN, which are utilized for membrane trafficking.
© 2010 John Wiley & Sons A/S.

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Year:  2010        PMID: 20874826      PMCID: PMC4906538          DOI: 10.1111/j.1600-0854.2010.01115.x

Source DB:  PubMed          Journal:  Traffic        ISSN: 1398-9219            Impact factor:   6.215


  32 in total

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Authors:  D Drecktrah; W J Brown
Journal:  Mol Biol Cell       Date:  1999-12       Impact factor: 4.138

2.  Membrane tubule-mediated reassembly and maintenance of the Golgi complex is disrupted by phospholipase A2 antagonists.

Authors:  P de Figueiredo; R S Polizotto; D Drecktrah; W J Brown
Journal:  Mol Biol Cell       Date:  1999-06       Impact factor: 4.138

3.  Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane.

Authors:  Carole L Baron; Vivek Malhotra
Journal:  Science       Date:  2001-11-29       Impact factor: 47.728

Review 4.  Membrane lipids and vesicular traffic.

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Journal:  Curr Opin Cell Biol       Date:  2004-08       Impact factor: 8.382

Review 5.  Phospholipase A2 (PLA2) enzymes in membrane trafficking: mediators of membrane shape and function.

Authors:  William J Brown; Kimberly Chambers; Anne Doody
Journal:  Traffic       Date:  2003-04       Impact factor: 6.215

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Journal:  Mol Biol Cell       Date:  2007-06-13       Impact factor: 4.138

7.  Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network.

Authors:  Charles Yeaman; M Inmaculada Ayala; Jessica R Wright; Frederic Bard; Carine Bossard; Agnes Ang; Yusuke Maeda; Thomas Seufferlein; Ira Mellman; W James Nelson; Vivek Malhotra
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8.  Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid.

Authors:  Edgar E Kooijman; Vladimir Chupin; Ben de Kruijff; Koert N J Burger
Journal:  Traffic       Date:  2003-03       Impact factor: 6.215

9.  The Cirque du Soleil of Golgi membrane dynamics.

Authors:  Vytas A Bankaitis
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Authors:  Maria Antonietta De Matteis; Anna Godi
Journal:  Nat Cell Biol       Date:  2004-06       Impact factor: 28.824

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  10 in total

Review 1.  Modular organization of the mammalian Golgi apparatus.

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Review 3.  A PLA1-2 punch regulates the Golgi complex.

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5.  Roles of acidic phospholipids and nucleotides in regulating membrane binding and activity of a calcium-independent phospholipase A2 isoform.

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6.  Disruption of Golgi morphology and altered protein glycosylation in PLA2G6-associated neurodegeneration.

Authors:  Mariska Davids; Megan S Kane; Miao He; Lynne A Wolfe; Xueli Li; Mohd A Raihan; Katherine R Chao; William P Bone; Cornelius F Boerkoel; William A Gahl; Camilo Toro
Journal:  J Med Genet       Date:  2015-12-14       Impact factor: 6.318

7.  Morpho-functional architecture of the Golgi complex of neuroendocrine cells.

Authors:  Emma Martínez-Alonso; Mónica Tomás; José A Martínez-Menárguez
Journal:  Front Endocrinol (Lausanne)       Date:  2013-03-28       Impact factor: 5.555

8.  Role of phospholipase A(2) in retrograde transport of ricin.

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9.  Lysophospholipids Facilitate COPII Vesicle Formation.

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10.  Gβ1γ2 activates phospholipase A2-dependent Golgi membrane tubule formation.

Authors:  Marie E Bechler; William J Brown
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  10 in total

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