Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking
about
Differential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2A walk-through of the yeast mating pheromone response pathwayThe structural basis for substrate and inhibitor selectivity of the anthrax lethal factorRegulation of WNK1 by an autoinhibitory domain and autophosphorylationIdentification of novel point mutations in ERK2 that selectively disrupt binding to MEK1ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1Adhesion stimulates direct PAK1/ERK2 association and leads to ERK-dependent PAK1 Thr212 phosphorylationRac-PAK signaling stimulates extracellular signal-regulated kinase (ERK) activation by regulating formation of MEK1-ERK complexesGIT1 is a novel MEK1-ERK1/2 scaffold that localizes to focal adhesionsA mitochondrial kinase complex is essential to mediate an ERK1/2-dependent phosphorylation of a key regulatory protein in steroid biosynthesis.Engineered single nucleotide polymorphisms in the mosquito MEK docking site alter Plasmodium berghei development in Anopheles gambiae.Different domains of the mitogen-activated protein kinases ERK3 and ERK2 direct subcellular localization and upstream specificity in vivo.Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity.Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446.Mechanisms of MAPK signalling specificity.Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo.An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors.Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions.Interaction with MEK causes nuclear export and downregulation of peroxisome proliferator-activated receptor gamma.Mapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking.MEK genomics in development and diseasePeptides targeting protein kinases: strategies and implications.Chromatin-bound mitogen-activated protein kinases transmit dynamic signals in transcription complexes in beta-cells.The roles of MAPKs in disease.Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a novel MAPK interaction motif.The D Domain of LRRC4 anchors ERK1/2 in the cytoplasm and competitively inhibits MEK/ERK activation in glioma cells.Molecular basis of MAP kinase regulation.Activation of the NaCl- and drought-induced RD29A and RD29B promoters by constitutively active Arabidopsis MAPKK or MAPK proteins.Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties.Binding of JNK/SAPK to MEKK1 is regulated by phosphorylation.Two clusters of residues at the docking groove of mitogen-activated protein kinases differentially mediate their functional interaction with the tyrosine phosphatases PTP-SL and STEP.Charged residues at protein interaction interfaces: unexpected conservation and orchestrated divergence.The transcriptional ETS2 repressor factor associates with active and inactive Erks through distinct FXF motifs.Anthrax lethal factor-cleavage products of MAPK (mitogen-activated protein kinase) kinases exhibit reduced binding to their cognate MAPKs.Tyrosine-specific MAPK phosphatases and the control of ERK signaling in PC12 cells.Atlantic salmon possess three mitogen activated protein kinase kinase 6 paralogs responding differently to stress.Identification of a C-terminal region that is required for the nuclear translocation of ERK2 by passive diffusion.PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.Docking interactions in the c-Jun N-terminal kinase pathway.Engineering and cytosolic delivery of a native regulatory protein and its variants for modulation of ERK2 signaling pathway.
P2860
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P2860
Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Hydrophobic as well as charged ...... rtant for their proper docking
@ast
Hydrophobic as well as charged ...... rtant for their proper docking
@en
Hydrophobic as well as charged ...... rtant for their proper docking
@nl
type
label
Hydrophobic as well as charged ...... rtant for their proper docking
@ast
Hydrophobic as well as charged ...... rtant for their proper docking
@en
Hydrophobic as well as charged ...... rtant for their proper docking
@nl
prefLabel
Hydrophobic as well as charged ...... rtant for their proper docking
@ast
Hydrophobic as well as charged ...... rtant for their proper docking
@en
Hydrophobic as well as charged ...... rtant for their proper docking
@nl
P2093
P2860
P356
P1476
Hydrophobic as well as charged ...... rtant for their proper docking
@en
P2093
P2860
P304
26509-26515
P356
10.1074/JBC.M102769200
P407
P577
2001-05-14T00:00:00Z