The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Ghrelin octanoylation mediated by an orphan lipid transferase
Open accessAbstract
The peptide hormone ghrelin is the only known protein modified with an O-linked octanoyl side group, which occurs on its third serine residue. This modification is crucial for ghrelin's physiological effects including regulation of feeding, adiposity, and insulin secretion. Despite the crucial role for octanoylation in the physiology of ghrelin, the lipid transferase that mediates this novel modification has remained unknown. Here we report the identification and characterization of human GOAT, the ghrelin O -acyl transferase. GOAT is a conserved orphan membrane-bound O -acyl transferase (MBOAT) that specifically octanoylates serine-3 of the ghrelin peptide. Transcripts for both GOAT and ghrelin occur predominantly in stomach and pancreas. GOAT is conserved across vertebrates, and genetic disruption of the GOAT gene in mice leads to complete absence of acylated ghrelin in circulation. The occurrence of ghrelin and GOAT in stomach and pancreas tissues demonstrates the relevance of GOAT in the acylation of ghrelin and further implicates acylated ghrelin in pancreatic function.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Ghrelin is a growth-hormone-releasing acylated peptide from stomach
Kojima, M., Hosoda, H., Date, Y., Nakazato, M., Matsuo, H., & Kangawa, K. (1999) · Nature · doi:10.1038/45230 · Cited by 8,479
Gastrointestinal regulation of food intake
Cummings, D. E., & Overduin, J. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30227 · Cited by 1,216
Biological, Physiological, Pathophysiological, and Pharmacological Aspects of Ghrelin
van der Lely, A. J., Tschöp, M., Heiman, M. L., & Ghigo, E. (2004) · Endocrine Reviews · doi:10.1210/er.2002-0029 · Cited by 1,187
A superfamily of membrane-bound O -acyltransferases with implications for Wnt signaling
Hofmann, K. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01539-x · Cited by 495
Cited by
Müller, T. D., Nogueiras, R., Andermann, M. L., Andrews, Z. B., Anker, S. D., Argente, J., Batterham, R. L., Benoit, S. C., Bowers, C. Y., Broglio, F., et al. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.03.005 · Cited by 1,034
Acyl‐coenzyme A:cholesterol acyltransferases
Chang, T.-Y., Li, B.-L., Chang, C. C. Y., & Urano, Y. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90926.2008 · Cited by 443
LEAP2 Is an Endogenous Antagonist of the Ghrelin Receptor
Ge, X., Yang, H., Bednarek, M. A., Galon-Tilleman, H., Chen, P., Chen, M., Lichtman, J. S., Wang, Y., Dalmas, O., Yin, Y., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.10.016 · Cited by 376
A healthy gastrointestinal microbiome is dependent on dietary diversity
Heiman, M. L., & Greenway, F. L. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.02.005 · Cited by 370
Single-nucleus and in situ RNA-sequencing reveal cell topographies in the human pancreas
Tosti, L., Hang, Y., Debnath, O., Tiesmeyer, S., Trefzer, T., Steiger, K., Ten, F. W., Lukassen, S., Ballke, S., Kühl, A. A., et al. (2021) · Gastroenterology · doi:10.1053/j.gastro.2020.11.010 · Cited by 228
Ghrelin regulation of glucose metabolism
Poher, A.-L., Tschöp, M. H., & Müller, T. D. (2018) · Peptides · doi:10.1016/j.peptides.2017.12.015 · Cited by 186
Spencer, S. J., Emmerzaal, T. L., Kozicz, T., & Andrews, Z. B. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.10.021 · Cited by 129
Current Understanding of the Hypothalamic Ghrelin Pathways Inducing Appetite and Adiposity
Al Massadi, O., López, M., Tschöp, M., Diéguez, C., & Nogueiras, R. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2016.12.003 · Cited by 124
Takagi, K., Legrand, R., Asakawa, A., Amitani, H., François, M., Tennoune, N., Coëffier, M., Claeyssens, S., do Rego, J.-C., Déchelotte, P., et al. (2013) · Nature Communications · doi:10.1038/ncomms3685 · Cited by 121
Rhea, E. M., Salameh, T. S., Gray, S., Niu, J., Banks, W. A., & Tong, J. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.09.007 · Cited by 114
Unraveling the role of the ghrelin gene peptides in the endocrine pancreas
Granata, R., Baragli, A., Settanni, F., Scarlatti, F., & Ghigo, E. (2010) · Journal of Molecular Endocrinology · doi:10.1677/jme-10-0019 · Cited by 97
The role of ghrelin in the regulation of glucose homeostasis
Alamri, B. N., Shin, K., Chappe, V., & Anini, Y. (2016) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2016-0018 · Cited by 93
Role of ghrelin in the pathophysiology of gastrointestinal disease
Cheung, C. K., & Wu, J. C.-Y. (2013) · Gut and Liver · doi:10.5009/gnl.2013.7.5.505 · Cited by 68
The neurological effects of ghrelin in brain diseases: Beyond metabolic functions
Jiao, Q., Du, X., Li, Y., Gong, B., Shi, L., Tang, T., & Jiang, H. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.12.010 · Cited by 62
Molecular mechanism of agonism and inverse agonism in ghrelin receptor
Qin, J., Cai, Y., Xu, Z., Ming, Q., Ji, S.-Y., Wu, C., Zhang, H., Mao, C., Shen, D.-D., Hirata, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-27975-9 · Cited by 57
Ghrelin-Mediated Hippocampal Neurogenesis: Implications for Health and Disease
Buntwal, L., Sassi, M., Morgan, A. H., Andrews, Z. B., & Davies, J. S. (2019) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2019.07.001 · Cited by 55
Stievenard, A., Méquinion, M., Andrews, Z. B., Destée, A., Chartier-Harlin, M.-C., Viltart, O., & Vanbesien-Mailliot, C. C. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.11.021 · Cited by 39
Davis, T. R., Pierce, M. R., Novak, S. X., & Hougland, J. L. (2021) · Open Biology · doi:10.1098/rsob.210080 · Cited by 33
“Proghrelin is uniquely O-octanoylated at the side chain of Ser-3 [1,3,5].”
BackgroundMethodInfluentialHornsby, A. K. E., Buntwal, L., Carisi, M. C., Santos, V. V., Johnston, F., Roberts, L. D., Sassi, M., Mequinion, M., Stark, R., Reichenbach, A., et al. (2020) · Cell Reports Medicine · doi:10.1016/j.xcrm.2020.100120 · Cited by 35
“UAG Inhibits Hippocampal Neurogenesis in Adult Mice To assess whether UAG regulates adult NSPC plasticity in the sub-granular zone (SGZ) of the hippocampus, we analyzed the effect of UAG administered peripherally for 7 days in WT and GOAT / mice.(23) GOAT / mice lack circulating acyl-ghrelin but have elevated levels o…”
MethodCarel, C., Marcoux, J., Réat, V., Parra, J., Latgé, G., Laval, F., Demange, P., Burlet-Schiltz, O., Milon, A., Daffé, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617888114 · Cited by 36
Ghrelin’s Role as a Major Regulator of Appetite and Its Other Functions in Neuroendocrinology
Lim, C. T., Kola, B., Korbonits, M., & Grossman, A. B. (2010) · Progress in Brain Research · doi:10.1016/s0079-6123(10)82008-4 · Cited by 34
Endocrine and Metabolic Actions of Ghrelin
Gasco, V., Beccuti, G., Marotta, F., Benso, A., Granata, R., Broglio, F., & Ghigo, E. (2010) · Endocrine Development · doi:10.1159/000262531 · Cited by 30
Rocking the MBOAT: Structural insights into the membrane bound O-acyltransferase family
Coupland, C. E., Ansell, T. B., Sansom, M. S. P., & Siebold, C. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102589 · Cited by 22
Teubner, B. J. W., Garretson, J. T., Hwang, Y., Cole, P. A., & Bartness, T. J. (2013) · Hormones and Behavior · doi:10.1016/j.yhbeh.2013.02.001 · Cited by 21
Acylation, a Conductor of Ghrelin Function in Brain Health and Disease
Thomas, A. S., Sassi, M., Angelini, R., Morgan, A. H., & Davies, J. S. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.831641 · Cited by 17
Metadata
- Authors
- Gutierrez, J. A., Solenberg, P. J., Perkins, D. R., Willency, J. A., Knierman, M. D., Jin, Z., Witcher, D. R., Luo, S., Onyia, J. E., & Hale, J. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-04-29
- Volume
- 105
- Issue
- 17
- Pages
- 6320-6325
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2107620313
- Cited by
- 803
- References
- 4
- FWCI
- 25.60
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
