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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-39DE-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CF58-8
Genre: Journal Article

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 Creators:
Galli, S., Author
Jahn, O., Author
Hitt, R., Author
Hesse, D., Author
Opitz, L., Author
Plessmann, U.1, Author              
Urlaub, H.1, Author              
Poderoso, J. J., Author
Jares-Erijman, E. A., Author
Jovin, T. M.2, Author              
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
2Emeritus Group Laboratory of Cellular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578629              

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 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.

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Language(s): eng - English
 Dates: 2009-10-22
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1371/journal.pone.0007541
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Title: PLoS One
Source Genre: Journal
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Pages: - Volume / Issue: 4 (10) Sequence Number: e7541 Start / End Page: - Identifier: -