Peptide mini-scaffold facilitates JNK3 activation in cells.

Zhan X, Stoy H, Kaoud TS, Perry NA, Chen Q, Perez A, Els-Heindl S, Slagis JV, Iverson TM, Beck-Sickinger AG, Gurevich EV, Dalby KN, Gurevich VV
Sci Rep. 2016 6: 21025

PMID: 26868142 · PMCID: PMC4751492 · DOI:10.1038/srep21025

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.

MeSH Terms (10)

Animals beta-Arrestin 1 beta-Arrestin 2 Cercopithecus aethiops COS Cells Enzyme Activation Enzyme Activators Humans Mitogen-Activated Protein Kinase 10 Peptides

Connections (3)

This publication is referenced by other Labnodes entities:

Links