Pull TAB1 to Activate

doi:10.1126/stke.2002.120.tw73

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Sci. STKE, 19 February 2002
Vol. 2002, Issue 120, p. tw73
[DOI: 10.1126/stke.2002.120.tw73]

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PROTEIN ACTIVATION Pull TAB1 to Activate

Members of the mitogen-activated protein kinase (MAPK) family control a wide range of cellular processes and are regulated as part of a cascade of protein kinases that are activated by sequential phosphorylation. Thus, MAPK kinases phosphorylate MAPKs on specific threonine and tyrosine residues, which leads to activation of the MAPK. Ge et al. (see the Perspective by Johnson) now show that there is another way to activate the so-called stress-activated MAPK known as p38 ${alpha}$ . They isolated proteins that interacted in a yeast system with human p38 ${alpha}$ and found TAB1 [transforming growth factor ß-activated protein kinase 1 (TAK1)-binding protein 1], a protein previously implicated in activating a different protein kinase, TAK1. TAB1 directly interacted with p38 ${alpha}$ and thereby enhanced autophosphorylation and activation of the p38 ${alpha}$ enzyme. Studies of signaling to p38 ${alpha}$ in cultured cells indicated that some stimuli activate p38 ${alpha}$ by the conventional kinase cascade, whereas others require the interaction with TAB1 and activation of p38 ${alpha}$ autophosphorylation.

B. Ge, H. Gram, F. Di Padova, B. Huang, L. New, R. J. Ulevitch, Y. Luo, J. Han, MAPKK-independent activation of p38 ${alpha}$ mediated by TAB1-dependent autophosphorylation of p38 ${alpha}$ . Science 295, 1291-1294 (2002). [Abstract] [Full Text]

G. Johnson, Scaffolding proteins--more than meets the eye. Science 295, 1249-1250 (2002). [Full Text]

Citation: Pull TAB1 to Activate. Sci. STKE 2002, tw73 (2002).