Journal
SCIENTIFIC REPORTS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep21025
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Funding
- NIH [GM077561, GM081756, EY011500, GM059802, CA167505, T32 GM008320]
- Cancer Prevention Research Institute of Texas (CPRIT) [RP140648]
- Welch Foundation [F-1390]
- DFG [SFB1052-A3]
- EU
- Free State of Saxony [ESF100148835]
- CPRIT
- DAAD RISE summer fellowship
- Vanderbilt International Scholars Program
- [GM095633]
- [NS065868]
- Office Of The Director
- Office Of Internatl Science &Engineering [1157751] Funding Source: National Science Foundation
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Three-kinase mitogen-activated protein kinase (MAPK) signaling cascades are present in virtually all eukaryotic cells. MAPK cascades are organized by scaffold proteins, which assemble cognate kinases into productive signaling complexes. Arrestin-3 facilitates JNK activation in cells, and a short 25-residue arrestin-3 peptide was identified as the critical JNK3-binding element. Here we demonstrate that this peptide also binds MKK4, MKK7, and ASK1, which are upstream JNK3-activating kinases. This peptide is sufficient to enhance JNK3 activity in cells. A homologous arrestin-2 peptide, which differs only in four positions, binds MKK4, but not MKK7 or JNK3, and is ineffective in cells at enhancing activation of JNK3. The arrestin-3 peptide is the smallest MAPK scaffold known. This peptide or its mimics can regulate MAPKs, affecting cellular decisions to live or die.
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