Scaffolding Proteins--More Than Meets the Eye
- 15 February 2002
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 295 (5558) , 1249-1250
- https://doi.org/10.1126/science.1069828
Abstract
The accepted pathway of MAPK activation is through a three kinase phosphorelay arrangement. However, as Johnson explains in his Perspective, new work has established an alternative way for a MAPK called p38a to be activated ( Ge et al.). Apparently, a scaffolding protein called TAB1 that is devoid of any known catalytic activity is able to interact with p38a, inducing its autophosphorylation and consequent activation.Keywords
This publication has 8 references indexed in Scilit:
- MAPKK-Independent Activation of p38α Mediated by TAB1-Dependent Autophosphorylation of p38αScience, 2002
- TAK1 is a ubiquitin-dependent kinase of MKK and IKKNature, 2001
- Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*Endocrine Reviews, 2001
- TAB2, a Novel Adaptor Protein, Mediates Activation of TAK1 MAPKKK by Linking TAK1 to TRAF6 in the IL-1 Signal Transduction PathwayMolecular Cell, 2000
- TAK1 Mitogen-activated Protein Kinase Kinase Kinase Is Activated by Autophosphorylation within Its Activation LoopJournal of Biological Chemistry, 2000
- Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to HumanPhysiological Reviews, 1999
- TAB1: An Activator of the TAK1 MAPKKK in TGF-β Signal TransductionScience, 1996
- Insulin-stimulated microtubule-associated protein kinase is phosphorylated on tyrosine and threonine in vivo.Proceedings of the National Academy of Sciences, 1988