• EN
  • DA

Danish NationalResearch Database

  • Publications
  • Researchers
Example Finds records
water{} containing the word "water".
water supplies"{}" containing the phrase "water supplies".
author:"Doe, John"author:"{}" containing the phrase "Doe, John" in the author field.
title:IEEEtitle:{} containing the word "IEEE" in the title field.
bech{} containing the word "bech".
marie bech"{}" containing the phrase "marie bech".
orcid:0000-0002-5429-5292orcid:{} Having a particular ORCID
Need more help? Advanced search tutorial
  • Selected (0)
  • History

Tissue specific phosphorylation of mitochondrial proteins isolated from rat liver, heart muscle, and skeletal muscle

    • Save to Mendeley
    • Export to BibTeX
    • Export to RIS
    • Email citation
Authors:
  • Bak, Steffen ;
    Close
    unknown
  • León, Ileana R ;
    Close
    unknown
  • Jensen, Ole Nørregaard ;
    Close
    Orcid logo0000-0003-1862-8528
    Department of Biochemistry and Molecular Biology, Faculty of Science, SDU
  • Højlund, Kurt
    Close
    Endocrinology, Department of Clinical Research, Faculty of Health Sciences, SDU
DOI:
10.1021/pr400281r
Abstract:
Phosphorylation of mitochondrial proteins in a variety of biological processes is increasingly being recognized and may contribute to the differences in function and energy demands observed in mitochondria from different tissues such as liver, heart, and skeletal muscle. Here, we used a combination of TiO2 phosphopeptide-enrichment, HILIC fractionation, and LC-MS/MS on isolated mitochondria to investigate the tissue-specific mitochondrial phosphoproteomes of rat liver, heart, and skeletal muscle. In total, we identified 899 phosphorylation sites in 354 different mitochondrial proteins including 479 potential novel sites. Most phosphorylation sites were detected in liver mitochondria (594), followed by heart (448) and skeletal muscle (336), and more phosphorylation sites were exclusively identified in liver mitochondria than in heart and skeletal muscle. Bioinformatics analysis pointed out enrichment for phosphoproteins involved in amino acid and fatty acid metabolism in liver mitochondria, whereas heart and skeletal muscle were enriched for phosphoproteins involved in energy metabolism, in particular, tricarboxylic acid cycle and oxidative phosphorylation. Multiple tissue-specific phosphorylation sites were identified in tissue-specific enzymes such as those encoded by HMGCS2, BDH1, PCK2, CPS1, and OTC in liver mitochondria, and CKMT2 and CPT1B in heart and skeletal muscle. Kinase prediction showed an important role for PKA and PKC in all tissues but also for proline-directed kinases in liver mitochondria. In conclusion, we provide a comprehensive map of mitochondrial phosphorylation sites, which covers approximately one-third of the mitochondrial proteome and can be targeted for the investigation of tissue-specific regulation of mitochondrial biological processes.
Type:
Journal article
Language:
English
Published in:
Journal of Proteome Research, 2013, Vol 12, Issue 10, p. 4327-39
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2013
Scientific Level:
Scientific
ID:
244617679

Full text access

  • Doi Get publisher edition via DOI resolver
Checking for on-site access...

On-site access

At institution

  • University southern denmark

Metrics

Feedback

Sitemap

  • Search
    • Statistics
    • Tutorial
    • Data
    • FAQ
    • Contact
  • About
    • Institutions
    • Release History
    • Cookies and Personal Data
  • Open Access
    • The Danish Open Access Indicator

Copyright © 1998–2018.

Fivu en