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  Extracellular MIF, but not its homologue D-DT, promotes fibroblast motility independent of its receptor CD74/CD44

Szczęśniak, P., Henke, T., Fröhlich, S., Plessmann, U., Urlaub, H., Leng, L., et al. (2021). Extracellular MIF, but not its homologue D-DT, promotes fibroblast motility independent of its receptor CD74/CD44. Journal of Cell Science, 134(3): jcs217356. doi:10.1242/jcs.217356.

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Szczęśniak, P., Author
Henke, T., Author
Fröhlich, S., Author
Plessmann, U.1, Author           
Urlaub, H.1, Author           
Leng, L., Author
Bucala, R., Author
Grosse, R., Author
Meinhardt, A., Author
Klug, J., Author
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1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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Free keywords: Macrophage migration inhibitory factor, MIF, D-dopachrome tautomerase, D-DT, MIF-2, Interactome, Actin cytoskeleton, CD74/CD44, Fibroblast motility, Chemokinesis
 Abstract: Macrophage migration inhibitory factor (MIF) and its homologue D-dopachrome tautomerase (D-DT) are widely expressed pro-inflammatory cytokines with chemokine-like functions that coordinate a wide spectrum of biological activities, such as migration. Here, we biotin-tagged intracellular MIF/D-DT in vivo to identify important cytosolic interactors and found a plethora of actin cytoskeleton-associated proteins. Although the receptor complex between CD74 and CD44 (CD74/CD44) is essential for signalling transduction in fibroblasts via extracellular MIF/D-DT, our interactome data suggested direct effects. We, thus, investigated whether MIF/D-DT can modulate cell migration independently of CD74/CD44. To distinguish between receptor- and non-receptor-mediated motility, we used fibroblasts that are either deficient or that express CD74/CD44 proteins, and treated them with recombinant MIF/D-DT. Interestingly, only MIF could stimulate chemokinesis in the presence or absence of CD74/CD44. The pro-migratory effects of MIF depended on lipid raft/caveolae-mediated but not clathrin-mediated endocytosis, on its tautomerase activity and, probably, on its thiol protein oxidoreductase activity. As MIF treatment restrained actin polymerisation in vitro, our findings establish a new intracellular role for MIF/D-DT in driving cell motility through modulation of the actin cytoskeleton.

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Language(s): eng - English
 Dates: 2021-02-102021-02
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1242/jcs.217356
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Title: Journal of Cell Science
Source Genre: Journal
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Pages: 12 Volume / Issue: 134 (3) Sequence Number: jcs217356 Start / End Page: - Identifier: ISSN: 1477-9137
ISSN: 0021-9533