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PAFAH Ib phospholipase A2 subunits have distinct roles in maintaining Golgi structure and function.

TitlePAFAH Ib phospholipase A2 subunits have distinct roles in maintaining Golgi structure and function.
Publication TypeJournal Article
Year of Publication2013
AuthorsBechler ME, Brown WJ
JournalBiochim Biophys Acta
Date Published2013 Mar
Keywords1-Alkyl-2-acetylglycerophosphocholine Esterase, Animals, Cattle, Cell Membrane, Cells, Cultured, Endoplasmic Reticulum, Gene Knockdown Techniques, Golgi Apparatus, Male, Microscopy, Electron, Microscopy, Fluorescence, Protein Kinase C, Protein Subunits, Protein Transport, RNA, Small Interfering, Secretory Pathway, Testis

Recent studies showed that the phospholipase subunits of Platelet Activating Factor Acetylhydrolase (PAFAH) Ib, α1 and α2 partially localize to the Golgi complex and regulate its structure and function. Using siRNA knockdown of individual subunits, we find that α1 and α2 perform overlapping and unique roles in regulating Golgi morphology, assembly, and secretory cargo trafficking. Knockdown of either α1 or α2 reduced secretion of soluble proteins, but neither single knockdown reduced secretion to the same degree as knockdown of both. Knockdown of α1 or α2 inhibited reassembly of an intact Golgi complex to the same extent as knockdown of both. Transport of VSV-G was slowed but at different steps in the secretory pathway: reduction of α1 slowed trans Golgi network to plasma membrane transport, whereas α2 loss reduced endoplasmic reticulum to Golgi trafficking. Similarly, knockdown of either subunit alone disrupted the Golgi complex but with markedly different morphologies. Finally, knockdown of α1, or double knockdown of α1 and α2, resulted in a significant redistribution of kinase dead protein kinase D from the Golgi to the plasma membrane, whereas loss of α2 alone had no such effect. These studies reveal an unexpected complexity in the regulation of Golgi structure and function by PAFAH Ib. This article is part of a Special Issue entitled Phospholipids and Phospholipid Metabolism.

Alternate JournalBiochim. Biophys. Acta
PubMed ID23262398
PubMed Central IDPMC4004371
Grant ListDK51596 / DK / NIDDK NIH HHS / United States
R01 GM101027 / GM / NIGMS NIH HHS / United States
R56 DK051596 / DK / NIDDK NIH HHS / United States
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