{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhou H"],"funding":["NIDDK NIH HHS","NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["3824-34"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1489000"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(10)"],"pubmed_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 p3"],"journal":["Molecular and cellular biology"],"pubmed_title":["Determinants that control the specific interactions between TAB1 and p38alpha."],"pmcid":["PMC1489000"],"funding_grant_id":["GM37696","R01 DK046993","P01 GM037696","DK46993","R01 AI041637","AI41637"],"pubmed_authors":["Goldsmith EJ","Lin S","Chen J","Zarubin T","Zheng M","Han J","Zhou H","Kolatkar AR","Akella R","Xie C","Ye Z"],"additional_accession":[]},"is_claimable":false,"name":"Determinants that control the specific interactions between TAB1 and p38alpha.","description":"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 p3","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 May","modification":"2026-05-01T10:49:18.716Z","creation":"2019-03-27T01:45:33Z"},"accession":"S-EPMC1489000","cross_references":{"pubmed":["16648477"],"doi":["10.1128/MCB.26.10.3824-3834.2006","10.1128/mcb.26.10.3824-3834.2006"]}}