Dimerization through the catalytic domain is essential for MEKK2 activation.
about
The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylationCHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic responseMip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation.JNK Signaling: Regulation and Functions Based on Complex Protein-Protein PartnershipsIdentification of MEKK2/3 serine phosphorylation site targeted by the Toll-like receptor and stress pathways.MEKK3 is essential for lymphopenia-induced T cell proliferation and survival.Development and validation of a high-throughput intrinsic ATPase activity assay for the discovery of MEKK2 inhibitors.Protein interactome analysis of 12 mitogen-activated protein kinase kinase kinase in rice using a yeast two-hybrid system.The cerebral cavernous malformation proteins CCM2L and CCM2 prevent the activation of the MAP kinase MEKK3.Homeostatic interactions between MEKK3 and TAK1 involved in NF-kappaB signalingOverexpression of MEKK2 is associated with colorectal carcinogenesis.Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.Oncogenic signaling of MEK5-ERK5.MEKK3 regulates IFN-gamma production in T cells through the Rac1/2-dependent MAPK cascades.Identification of ponatinib and other known kinase inhibitors with potent MEKK2 inhibitory activity.Protein interface remodeling in a chemically induced protein dimer.Noncanonical function of MEKK2 and MEK5 PB1 domains for coordinated extracellular signal-regulated kinase 5 and c-Jun N-terminal kinase signaling.Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form.MEKK2 kinase association with 14-3-3 protein regulates activation of c-Jun N-terminal kinase.Dimerization in protein kinase signaling.Homo- and hetero-oligomerization of beta-arrestins in living cells.Discovery and characterization of an iminocoumarin scaffold as an inhibitor of MEKK2 (MAP3K2).
P2860
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P2860
Dimerization through the catalytic domain is essential for MEKK2 activation.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Dimerization through the catalytic domain is essential for MEKK2 activation.
@en
type
label
Dimerization through the catalytic domain is essential for MEKK2 activation.
@en
prefLabel
Dimerization through the catalytic domain is essential for MEKK2 activation.
@en
P2093
P2860
P356
P1476
Dimerization through the catalytic domain is essential for MEKK2 activation.
@en
P2093
David Spencer
Dongyu Zhang
Jinke Cheng
Qiaojia Huang
P2860
P304
13477-13482
P356
10.1074/JBC.M414258200
P407
P577
2005-02-04T00:00:00Z