PubMed:12167088 JSONTXT

{"project":"LocText","denotations":[{"id":"T1","span":{"begin":57,"end":60},"obj":"uniprot:O60239"},{"id":"T2","span":{"begin":62,"end":68},"obj":"uniprot:O60239"},{"id":"T3","span":{"begin":87,"end":99},"obj":"go:GO:0005739"},{"id":"T4","span":{"begin":179,"end":182},"obj":"uniprot:O60239"},{"id":"T5","span":{"begin":187,"end":192},"obj":"taxonomy:4932"},{"id":"T6","span":{"begin":215,"end":218},"obj":"uniprot:O60239"},{"id":"T7","span":{"begin":349,"end":373},"obj":"uniprot:uniprot:"},{"id":"T8","span":{"begin":375,"end":378},"obj":"uniprot:uniprot:"},{"id":"T9","span":{"begin":411,"end":414},"obj":"uniprot:O60239"},{"id":"T10","span":{"begin":566,"end":571},"obj":"uniprot:uniprot:"},{"id":"T11","span":{"begin":787,"end":790},"obj":"uniprot:O60239"},{"id":"T12","span":{"begin":839,"end":844},"obj":"uniprot:uniprot:"},{"id":"T13","span":{"begin":893,"end":896},"obj":"uniprot:O60239"},{"id":"T14","span":{"begin":1003,"end":1006},"obj":"uniprot:O60239"},{"id":"T15","span":{"begin":1026,"end":1038},"obj":"go:GO:0005739"},{"id":"T16","span":{"begin":1137,"end":1140},"obj":"uniprot:O60239"},{"id":"T17","span":{"begin":1254,"end":1257},"obj":"uniprot:uniprot:"}],"relations":[{"id":"R1","pred":"localizeTo","subj":"T1","obj":"T3"},{"id":"R2","pred":"localizeTo","subj":"T2","obj":"T3"},{"id":"R3","pred":"localizeTo","subj":"T14","obj":"T15"}],"namespaces":[{"prefix":"uniprot","uri":"http://identifiers.org/uniprot/"},{"prefix":"taxonomy","uri":"http://identifiers.org/taxonomy/"},{"prefix":"go","uri":"http://identifiers.org/go/"}],"text":"A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondria.\nWe have identified a novel c-Jun N-terminal kinase (JNK)-interacting protein, Sab, by yeast two-hybrid screening. Sab binds to and serves as a substrate for JNK in vitro, and was previously found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule. Using deletion and site-directed mutagenesis, we demonstrate that the most N-terminal KIM in Sab is essential for JNK binding, and that, as with c-Jun, physical interaction with JNK is necessary for Sab phosphorylation. Interestingly, confocal immunocytochemistry and cell fractionation studies indicate that Sab is associated with mitochondria, where it co-localizes with a fraction of active JNK. These and previously reported properties of Sab suggest a possible role in targeting JNK to this subcellular compartment and/or mediating cross-talk between the Btk and JNK signal transduction pathways."}