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Journal Article

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

MPS-Authors
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Plessmann,  U.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Jovin,  T. M.
Emeritus Group Laboratory of Cellular Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

1922342.pdf
(Publisher version), 2MB

Supplementary Material (public)

1922342-Suppl-1-15.zip
(Supplementary material), 15MB

Citation

Galli, S., Jahn, O., Hitt, R., Hesse, D., Opitz, L., Plessmann, U., et al. (2009). A new paradigm for MAPK: Structural interactions of hERK1 with mitochondria in HeLa cells. PLoS One, 4(10): e7541. doi:10.1371/journal.pone.0007541.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-39DE-3
Abstract
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.