ArticleMolecular biology of the cell2011
The phospholipase A₂ enzyme complex PAFAH Ib mediates endosomal membrane tubule formation and trafficking.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- The Interplay between Retinal Pathways of Cholesterol Output and Its Effects on Mouse Retina.Biomolecules · 2019Article
- Methods for analyzing the role of phospholipase A₂ enzymes in endosome membrane tubule formation.Methods in cell biology · 2015Article
- Insulin-regulated protein palmitoylation impacts endothelial cell function.Arteriosclerosis, thrombosis, and vascular biology · 2014Article
- PAFAH Ib phospholipase A2 subunits have distinct roles in maintaining Golgi structure and function.Biochimica et biophysica acta · 2013Article
- RNAi-based functional profiling of loci from blood lipid genome-wide association studies identifies genes with cholesterol-regulatory function.PLoS genetics · 2013Article
- Loss of PAFAH1B2 reduces amyloid-β generation by promoting the degradation of amyloid precursor protein C-terminal fragments.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Regulation of the Golgi complex by phospholipid remodeling enzymes.Biochimica et biophysica acta · 2012Review
- cPLA2α and EHD1 interact and regulate the vesiculation of cholesterol-rich, GPI-anchored, protein-containing endosomes.Molecular biology of the cell · 2012Article
- A PLA1-2 punch regulates the Golgi complex.Trends in cell biology · 2012Review
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies have shown that membrane tubule-mediated export from endosomal compartments requires a cytoplasmic phospholipase A(2) (PLA(2)) activity. Here we report that the cytoplasmic PLA(2) enzyme complex platelet-activating factor acetylhydrolase (PAFAH) Ib, which consists of α1, α2, and LIS1 subunits, regulates the distribution and function of endosomes. The catalytic subunits α1 and α2 are located on early-sorting endosomes and the central endocytic recycling compartment (ERC) and their overexpression, but not overexpression of their catalytically inactive counterparts, induced endosome membrane tubules. In addition, overexpression α1 and α2 altered normal endocytic trafficking; transferrin was recycled back to the plasma membrane directly from peripheral early-sorting endosomes instead of making an intermediate stop in the ERC. Consistent with these results, small interfering RNA-mediated knockdown of α1 and α2 significantly inhibited the formation of endosome membrane tubules and delayed the recycling of transferrin. In addition, the results agree with previous reports that PAFAH Ib α1 and α2 expression levels affect the distribution of endosomes within the cell through interactions with the dynein regulator LIS1. These studies show that PAFAH Ib regulates endocytic membrane trafficking through novel mechanisms involving both PLA(2) activity and LIS1-dependent dynein function.
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