ArticleBiochemical and biophysical research communications2010
Membrane topology of human AGPAT3 (LPAAT3).
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- The Emerging Role of LPA as an Oncometabolite.Cells · 2024Review
- A loss of function variant in AGPAT3 underlies intellectual disability and retinitis pigmentosa (IDRP) syndrome.European journal of human genetics : EJHG · 2023Article
- Tetra-linoleoyl cardiolipin depletion plays a major role in the pathogenesis of sarcopenia.Medical hypotheses · 2019Article
- Analysis of miRNA-seq in the liver of common carp (Cyprinus carpio L.) in response to different environmental temperatures.Functional & integrative genomics · 2019Article
- The Structure and Function of Acylglycerophosphate Acyltransferase 4/ Lysophosphatidic Acid Acyltransferase Delta (AGPAT4/LPAATδ).Frontiers in cell and developmental biology · 2019Review
- Effects of aqueous extract of Arctium lappa L. roots on serum lipid metabolism.The Journal of international medical research · 2018Article
- How lipid droplets "TAG" along: Glycerolipid synthetic enzymes and lipid storage.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer.Nature structural & molecular biology · 2017Article
- CCTOP: a Consensus Constrained TOPology prediction web server.Nucleic acids research · 2015Article
- Disorders of phospholipid metabolism: an emerging class of mitochondrial disease due to defects in nuclear genes.Frontiers in genetics · 2015Review
- Identification and characterization of a gene encoding a putative lysophosphatidyl acyltransferase from Arachis hypogaea.Journal of biosciences · 2012Article
- Regulation of the Golgi complex by phospholipid remodeling enzymes.Biochimica et biophysica acta · 2012Review
- Common variation in fatty acid genes and resuscitation from sudden cardiac arrest.Circulation. Cardiovascular genetics · 2012Article
- Topology of 1-acyl-sn-glycerol-3-phosphate acyltransferases SLC1 and ALE1 and related membrane-bound O-acyltransferases (MBOATs) of Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- Mammalian triacylglycerol metabolism: synthesis, lipolysis, and signaling.Chemical reviews · 2011Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Integral membrane lysophospholipid acyltransferases (AT) are involved in many reactions that produce phospholipids and triglycerides. Enzymes that utilize lysophosphatidic acid (LPA) as an acceptor substrate have been termed LPAATs, and several are members of the 1-acylglycerol-3-phosphate O-acyltransferase (AGPAT) gene family. Amino acid sequence comparisons with other acyltransferases reveal that AGPATs contain four conserved motifs (I-IV), whose invariant residues appear to be important for catalysis and/or substrate recognition. Although the enzymatic activities of many AGPATs are known, for many members their structural organization within membranes and their exact biological functions are unclear. Recently, a new function for AGPATs was discovered when it was determined that human AGPAT3/LPAAT3 is involved in the structure and function of the Golgi complex. Here we have determined the topological orientation of human AGPAT3/LPAAT3. AGPAT3/LPAAT3 possesses two transmembrane domains, one of which separates motifs I and II, which are thought to form a functional unit that is critical for enzymatic activity. This is a surprising result but similar to a recent study on the topology of human LPAAT 1. The data is consistent with a structural arrangement in which motif I is located in the cytoplasm and motif II is in the endoplasmic reticulum and Golgi lumen, suggesting a different model for AGPAT3/LPAAT3's enzymatic mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.