TY - JOUR
T1 - MEKK1 binds Raf-1 and the ERK2 cascade components
AU - Karandikar, Mahesh
AU - Xu, Shuichan
AU - Cobb, Melanie H.
PY - 2000/12/22
Y1 - 2000/12/22
N2 - Mitogen-activated protein (MAP) kinase caseades are involed in transmitting signals that are generated at the cell surface into the cytosol and nucleus and consist of three sequentially acting enzymes: a MAP kinase, an upstream MAP/extracellular signal-regulated protein kinase (ERK) kinase (MEK), and a MEK kinase (MEKK). Protein-protein interactions within these cascades provide a mechanism to control the localization and function of the protiens. MEKK1 is implicated in activation of the c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) and ERK1/2 MAP kinase pathways. We showed previously that MEKK1 binds directly to JNK/SAPK. In this study we demonstrate that endogenous MEKK1 binds to endogenous ERK2, MEK1, and another MEKK level kinase, Raf-1, suggesting that it can assemble all three proteins of the ERK2 MAP kinase module.
AB - Mitogen-activated protein (MAP) kinase caseades are involed in transmitting signals that are generated at the cell surface into the cytosol and nucleus and consist of three sequentially acting enzymes: a MAP kinase, an upstream MAP/extracellular signal-regulated protein kinase (ERK) kinase (MEK), and a MEK kinase (MEKK). Protein-protein interactions within these cascades provide a mechanism to control the localization and function of the protiens. MEKK1 is implicated in activation of the c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) and ERK1/2 MAP kinase pathways. We showed previously that MEKK1 binds directly to JNK/SAPK. In this study we demonstrate that endogenous MEKK1 binds to endogenous ERK2, MEK1, and another MEKK level kinase, Raf-1, suggesting that it can assemble all three proteins of the ERK2 MAP kinase module.
UR - http://www.scopus.com/inward/record.url?scp=0034704153&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034704153&partnerID=8YFLogxK
U2 - 10.1074/jbc.M005926200
DO - 10.1074/jbc.M005926200
M3 - Article
C2 - 10969079
AN - SCOPUS:0034704153
SN - 0021-9258
VL - 275
SP - 40120
EP - 40127
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 51
ER -