ArticleThe Journal of biological chemistry2013
Architectural organization of the metabolic regulatory enzyme ghrelin O-acyltransferase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 65 citations in OpenAlex.
- Therapeutic potential of ghrelin/GOAT/GHSR system in gastrointestinal disorders.Frontiers in nutrition · 2024Review
- Combined Computational-Biochemical Approach Offers an Accelerated Path to Membrane Protein Solubilization.Journal of chemical information and modeling · 2023Article
- Cellular Uptake of a Fluorescent Ligand Reveals GhrelinACS chemical biology · 2023Article
- A rising tide lifts all MBOATs: recent progress in structural and functional understanding of membrane boundFrontiers in physiology · 2023Review
- Access and utilization of long chain fatty acyl-CoA by zDHHC protein acyltransferases.Current opinion in structural biology · 2022Review
- Roles of Ghrelin and Leptin in Body Mass Regulation under Food Restriction Based on the AMPK Pathway in the Red-Backed Vole,Animals : an open access journal from MDPI · 2022Article
- Discovery of novel inhibitors of ghrelin O-acyltransferase enzyme: anResearch in pharmaceutical sciences · 2022Article
- Acylation, a Conductor of Ghrelin Function in Brain Health and Disease.Frontiers in physiology · 2022Review
- From "Hunger Hormone" to "It's Complicated": Ghrelin Beyond Feeding Control.Physiology (Bethesda, Md.) · 2022Review
- In Search of Small Molecules That Selectively Inhibit MBOAT4.Molecules (Basel, Switzerland) · 2021Article
- Ghrelin octanoylation by ghrelinOpen biology · 2021Review
- Determination of the membrane topology of PORCN, an O-acyl transferase that modifies Wnt signalling proteins.Open biology · 2021Article
- An overview of ghrelinExpert opinion on therapeutic patents · 2020Review
- Ghrelin Signaling: GOAT and GHS-R1a Take a LEAP in Complexity.Trends in endocrinology and metabolism: TEM · 2020Review
- Hedgehog Acyltransferase Promotes Uptake of Palmitoyl-CoA across the Endoplasmic Reticulum Membrane.Cell reports · 2019Article
- The ghrelinThe Journal of biological chemistry · 2019Article
- Article
- A partial reconstitution implicates DltD in catalyzing lipoteichoic acid d-alanylation.The Journal of biological chemistry · 2018Article
- Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
Abstract
Ghrelin O-acyltransferase (GOAT) is a polytopic integral membrane protein required for activation of ghrelin, a secreted metabolism-regulating peptide hormone. Although GOAT is a potential therapeutic target for the treatment of obesity and diabetes and plays a key role in other physiologic processes, little is known about its structure or mechanism. GOAT is a member of the membrane-bound O-acyltransferase (MBOAT) family, a group of polytopic integral membrane proteins involved in lipid-biosynthetic and lipid-signaling reactions from prokaryotes to humans. Here we use phylogeny and a variety of bioinformatic tools to predict the topology of GOAT. Using selective permeabilization indirect immunofluorescence microscopy in combination with glycosylation shift immunoblotting, we demonstrate that GOAT contains 11 transmembrane helices and one reentrant loop. Development of the V5Glyc tag, a novel, small, and sensitive dual topology reporter, facilitated these experiments. The MBOAT family invariant residue His-338 is in the ER lumen, consistent with other family members, but conserved Asn-307 is cytosolic, making it unlikely that both are involved in catalysis. Photocross-linking of synthetic ghrelin analogs and inhibitors demonstrates binding to the C-terminal region of GOAT, consistent with a role of His-338 in the active site. This knowledge of GOAT architecture is important for a deeper understanding of the mechanism of GOAT and other MBOATs and could ultimately advance the discovery of selective inhibitors for these enzymes.
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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.