Identification of serine phosphorylation in mitochondrial uncoupling protein 1
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Native uncoupling protein 1 was purified from rat brown adipose tissue of cold-acclimated rats and rats kept at room temperature, in the presence of phosphatase inhibitors. The purified protein from cold-acclimated animals was digested with trypsin and immobilized metal affinity chromatography was used to select for phosphopeptides. Tandem mass spectroscopic analysis of the peptides derived from uncoupling protein 1, suggests phosphorylation of serine 3 or 4 and identified phosphorylation of serine 51. Furthermore, we were able to demonstrate that antibodies to phosphoserine detect full-length UCP 1 and that the proportion of phosphoserine on UCP1, purified from cold-acclimated rats, was significantly greater than that on UCP 1 from rats kept at room temperature (90+/-4% compared to 62+/-8%, p=0.013), respectively). We conclude that uncoupling protein 1 is a phosphoprotein and that cold-acclimation increases the proportion of UCP1 that is serine phosphorylated.
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UCP-1 activity is modulated by phosphorylation, which increases in response to cold in rats.
“In addition, UCP-1 activity is also tightly modulated by phosphorylation, a phenomenon shown to increase in response to cold in rats [10].”
From Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases (2019) · cites this paper as [10]
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Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases
Demine, S., Renard, P., & Arnould, T. (2019) · Cells · doi:10.3390/cells8080795 · Cited by 476 · see citing works
“In addition, UCP-1 activity is also tightly modulated by phosphorylation, a phenomenon shown to increase in response to cold in rats [10].”
BackgroundGlutathionylation Acts as a Control Switch for Uncoupling Proteins UCP2 and UCP3
Mailloux, R. J., Seifert, E. L., Bouillaud, F., Aguer, C., Collins, S., & Harper, M.-E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.240242 · Cited by 174 · see citing works
- Authors
- Carroll, A. M., Porter, R. K., & Morrice, N. A.
- Affiliations
- Trinity College Dublin (IE)
- University of Dundee (GB)
- Corresponding author
- Morrice, Nick A.
- ORCID
- Porter, Richard K.
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 1777
- Issue
- 7-8
- Pages
- 1060-1065
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2006922404
- Cited by
- 26
- References
- 33
- Citations by year
- 2024: 1 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 4 · 2016: 1 · 2015: 1 · 2013: 1 · 2012: 2
- FWCI
- 2.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Science Foundation Ireland
- Engineering and Physical Sciences Research Council
- Biotechnology and Biological Sciences Research Council
- Topics
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- UCP1, serine phosphorylation, brown adipose tissue, cold acclimation, phosphoproteins, phosphoserine, thermogenesis, phosphorylation sites
- MeSH terms
- Acclimatization, Uncoupling Protein 1, Animals, Body Temperature Regulation, Adipose Tissue, Brown, Cold Temperature, Ion Channels, Mammals, Mitochondria, Phosphoric Monoester Hydrolases, Phosphoproteins, Phosphorylation, Serine, Rats, Wistar, Mitochondrial Proteins, Rats
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