A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells

• Published in: PloS one 2009-10, Vol.4 (10), p.e7541-e7541
• Main Authors: Galli, Soledad, Jahn, Olaf, Hitt, Reiner, Hesse, Doerte, Opitz, Lennart, Plessmann, Uwe, Urlaub, Henning, Poderoso, Juan Jose, Jares-Erijman, Elizabeth A, Jovin, Thomas M
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Arabidopsis; Automation; Biochemistry; Biochemistry/Cell Signaling and Trafficking Structures; Biochemistry/Chemical Biology of the Cell; Cell Biology/Cell Growth and Division; Cell Biology/Cell Signaling; Cell Biology/Chemical Biology of the Cell; Cell Proliferation; Chemical Biology/Chemical Biology of the Cell; Chemical Biology/Protein Chemistry and Proteomics; Chemistry/Biochemistry; Cholera; Defense mechanisms; DNA binding proteins; Experiments; Extracellular signal-regulated kinase; Gene expression; Gene Expression Profiling; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Neoplastic; Glutathione Transferase - metabolism; HeLa Cells; Histones; Humans; Kinases; Laboratories; Localization; MAP kinase; MAP Kinase Signaling System; Mass spectrometry; Metabolism; Microscopy; Mitochondria; Mitochondria - metabolism; Mitogen-Activated Protein Kinase 3 - metabolism; Molecular Sequence Data; Phosphorylation; Physiological aspects; Protein kinase; Protein kinases; Proteins; Proteomics; Proteomics - methods; Scientific imaging; Sequence Homology, Amino Acid; Signal transduction; Signaling; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Transcription factors
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0007541

Extracellular signal-regulated protein kinase 1 and 2 (ERK1/2) are members of the MAPK family and participate in the transduction of stimuli in cellular responses. Their long-term actions are accomplished by promoting the expression of specific genes whereas faster responses are achieved by direct phosphorylation of downstream effectors located throughout the cell. In this study we determined that hERK1 translocates to the mitochondria of HeLa cells upon a proliferative stimulus. In the mitochondrial environment, hERK1 physically associates with (i) at least 5 mitochondrial proteins with functions related to transport (i.e. VDAC1), signalling, and metabolism; (ii) histones H2A and H4; and (iii) other cytosolic proteins. This work indicates for the first time the presence of diverse ERK-complexes in mitochondria and thus provides a new perspective for assessing the functions of ERK1 in the regulation of cellular signalling and trafficking in HeLa cells.