ArticleMolecular and cellular biology2006
Determinants that control the specific interactions between TAB1 and p38alpha.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Fluorescence resonance energy transfer (FRET) spatiotemporal mapping of atypical P38 reveals an endosomal and cytosolic spatial bias.Scientific reports · 2023Article
- Atypical p38 Signaling, Activation, and Implications for Disease.International journal of molecular sciences · 2021Review
- The p38 Pathway: From Biology to Cancer Therapy.International journal of molecular sciences · 2020Review
- The TAB1-p38α complex aggravates myocardial injury and can be targeted by small molecules.JCI insight · 2018Article
- Anti-proliferative Effect of C3 Exoenzyme in Fibroblasts is Mediated by c-Jun Phosphorylation.Journal of molecular signaling · 2017Article
- Ubiquitin plays an atypical role in GPCR-induced p38 MAP kinase activation on endosomes.The Journal of cell biology · 2015Article
- The Gβγ-Src signaling pathway regulates TNF-induced necroptosis via control of necrosome translocation.Cell research · 2014Article
- Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death.Cell research · 2014Article
- Mechanism and consequence of the autoactivation of p38α mitogen-activated protein kinase promoted by TAB1.Nature structural & molecular biology · 2013Article
- Disruption of TAB1/p38α interaction using a cell-permeable peptide limits myocardial ischemia/reperfusion injury.Molecular therapy : the journal of the American Society of Gene Therapy · 2013Article
- Structural mechanisms of allostery and autoinhibition in JNK family kinases.Structure (London, England : 1993) · 2012Article
- Article
- Heat shock protein 27 mediated signaling in viral infection.Biochemistry · 2012Article
- Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.PloS one · 2011Article
- Amyloidogenic light chains induce cardiomyocyte contractile dysfunction and apoptosis via a non-canonical p38alpha MAPK pathway.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Hydrogen-exchange mass spectrometry reveals activation-induced changes in the conformational mobility of p38alpha MAP kinase.Journal of molecular biology · 2008Article
- Substrate and docking interactions in serine/threonine protein kinases.Chemical reviews · 2007Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Previous studies have revealed that transforming growth factor-beta-activated protein kinase 1 (TAB1) interacts with p38alpha and induces p38alpha autophosphorylation. Here, we examine the sequence requirements in TAB1 and p38alpha that drive their interaction. Deletion and point mutations in TAB1 reveal that a proline residue in the C terminus of TAB1 (Pro412) is necessary for its interaction with p38alpha. Furthermore, a cryptic D-domain-like docking site was identified adjacent to the N terminus of Pro412, putting Pro412 in the phi(B)+3 position of the docking site. Through mutational analysis, we found that the previously identified hydrophobic docking groove in p38alpha is involved in this interaction, whereas the CD domain and ED domain are not. Furthermore, chimeric analysis with p38beta (which does not bind to TAB1) revealed a previously unidentified locus of p38alpha comprising Thr218 and Ile275 that is essential for specific binding of p38alpha to TAB1. Converting either of these residues to the corresponding amino acid of p38beta abolishes p38alpha interaction with TAB1. These p38alpha mutants still can be fully activated by p38alpha upstream activating kinase mitogen-activated protein kinase kinase 6, but their basal activity and activation in response to some extracellular stimuli are reduced. Adjacent to Thr218 and Ile275 is a site where large conformational changes occur in the presence of docking-site peptides derived from p38alpha substrates and activators. This suggests that TAB1-induced autophosphorylation of p38alpha results from conformational changes that are similar but unique to those seen in p38alpha interactions with its substrates and activating kinases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.