Identification and characterization of functional domains in a mixed lineage kinase LZK

FEBS Letters

Masaki, Megumi¹  Ikeda, Atsushi¹  Kozutsumi, Yasunori¹  Kawasaki, Toshisuke¹  Oka, Shogo¹ 

[1] Department of Biological Chemistry and CREST (Core Research for Educational Science and Technology) Project, Japan Science and Technology Corporation, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan

关键词: Signal transduction;    Mixed lineage kinase;    c-Jun NH2 terminal kinase;    Stress-activated protein kinase;    Mitogen-activated protein kinase;    Leucine zipper;    MLK;    mixed lineage kinase;    LZK;    leucine zipper-bearing kinase;    JNK;    c-Jun NH2 terminal kinase;    MAPK;    mitogen-activated protein kinase;    MAPKK;    MAPK kinase;    MAPKKK;    MAPKK kinase;    MEKK1;    mitogen-activated protein or extracellular signal-regulated protein kinase kinase kinase 1;    MUK;    MAPK-upstream kinase;    DLK;    dual leucine zipper-bearing kinase;    ASK1;    apoptosis signal-regulated kinase 1;    HA;    hemagglutinin;    GST;    glutathione S-transferase;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(00)02432-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The mixed lineage kinase (MLK) family is a recently described protein kinase family. The MLKs contain a kinase domain followed by a dual leucine zipper-like motif. We previously reported the molecular cloning of LZK (eucine ipper-bearing inase), a novel MLK, and that LZK activated the c-Jun NH₂ terminal kinase (JNK)/stress-activated protein kinase (SAPK) pathway through MKK7 in cells. Here, we reveal that LZK forms dimers/oligomers through its dual leucine zipper-like motif, and that this is necessary for activation of the JNK/SAPK pathway. We also identify the C-terminal functional region of LZK, which is indispensable for the activation of SEK1, but not that of MKK7.

【 授权许可】

Unknown