A role for phospholipase D3 in myotube formation

Phospholipase D3 (PLD3) is a non-classical, poorly characterized member of the PLD superfamily of signaling enzymes. PLD3 is a type II glycoprotein associated with the endoplasmic reticulum, is expressed in a wide range of tissues and cells, and undergoes dramatic upregulation in neurons and muscle...

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Bibliographic Details
Published in:PloS one 2012-03, Vol.7 (3), p.e33341-e33341
Main Authors: Osisami, Mary, Ali, Wahida, Frohman, Michael A
Format: Article
Language:English
Subjects:
Analysis of Variance
Animals
Biology
Biosynthesis
Blotting, Western
Cell cycle
Cell Differentiation - physiology
Deoxyribonucleic acid
Differentiation
DNA
DNA Primers - genetics
Endoplasmic reticulum
Endoplasmic Reticulum - enzymology
Endoplasmic Reticulum - physiology
Enzymes
Gene expression
Glycoproteins
Lipids
Mammals
Mice
Microscopy, Fluorescence
Muscle Fibers, Skeletal - enzymology
Muscle Fibers, Skeletal - physiology
Muscles
Myogenesis
Myotubes
NIH 3T3 Cells
Phospholipase
Phospholipase D
Phospholipase D - genetics
Phospholipase D - metabolism
Phospholipases
Plasmids - genetics
Proteins
Real-Time Polymerase Chain Reaction
Rodents
Signaling
Skeletal muscle
Tethering
Tissues
Transcription factors
Transfection
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Summary:Phospholipase D3 (PLD3) is a non-classical, poorly characterized member of the PLD superfamily of signaling enzymes. PLD3 is a type II glycoprotein associated with the endoplasmic reticulum, is expressed in a wide range of tissues and cells, and undergoes dramatic upregulation in neurons and muscle cells during differentiation. Using an in vitro skeletal muscle differentiation system, we define the ER-tethering mechanism and report that increased PLD3 expression enhances myotube formation, whereas a putatively dominant-negative PLD3 mutant isoform reduces myotube formation. ER stress, which also enhances myotube formation, is shown here to increase PLD3 expression levels. PLD3 protein was observed to localize to a restricted set of subcellular membrane sites in myotubes that may derive from or constitute a subdomain of the endoplasmic reticulum. These findings suggest that PLD3 plays a role in myogenesis during myotube formation, potentially in the events surrounding ER reorganization.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0033341