Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain

Domenico De Rasmo, Giuseppe Palmisano, Salvatore Scacco, Zuzana Technikova-Dobrova, Damiano Panelli, Tiziana Cocco, Anna Maria Sardanelli, Antonio Gnoni, Loris Micelli, Antonio Trani, Aldo Di Luccia, Sergio Papa

Research output: Contribution to journalArticle

Abstract

The NDUFS4 subunit of complex I of the mammalian respiratory chain has a fully conserved carboxy-terminus with a canonical RVSTK phosphorylation site. Immunochemical analysis with specific antibodies shows that the serine in this site of the protein is natively present in complex I in both the phosphorylated and non-phosphorylated state. Two-dimensional IEF/SDS-PAGE electrophoresis, 32P labelling and immunodetection show that " in vitro" PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I. 32P labelling and TLC phosphoaminoacid mapping show that PKA phosphorylates serine and threonine residues in the purified heterologous human NDUFS4 protein.

Original languageEnglish
Pages (from-to)464-471
Number of pages8
JournalMitochondrion
Volume10
Issue number5
DOIs
Publication statusPublished - Aug 2010

Keywords

  • CAMP-dependent protein kinase
  • Complex I
  • Mitochondrial phosphoproteins
  • NDUFS4 phosphorylation

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Molecular Medicine

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  • Cite this

    Rasmo, D. D., Palmisano, G., Scacco, S., Technikova-Dobrova, Z., Panelli, D., Cocco, T., Sardanelli, A. M., Gnoni, A., Micelli, L., Trani, A., Luccia, A. D., & Papa, S. (2010). Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain. Mitochondrion, 10(5), 464-471. https://doi.org/10.1016/j.mito.2010.04.005