PMID- 10655591
OWN - NLM
STAT- MEDLINE
DCOM- 20000320
LR  - 20220817
IS  - 1465-7392 (Print)
IS  - 1465-7392 (Linking)
VI  - 2
IP  - 2
DP  - 2000 Feb
TI  - A conserved docking motif in MAP kinases common to substrates, activators and 
      regulators.
PG  - 110-6
AB  - Mitogen-activated protein kinases (MAPKs) are specifically phosphorylated and 
      activated by the MAPK kinases, phosphorylate various targets such as 
      MAPK-activated protein kinases and transcription factors, and are inactivated by 
      specific phosphatases. Recently, docking interactions via the non-catalytic 
      regions of MAPKs have been suggested to be important in regulating these 
      reactions. Here we identify docking sites in MAPKs and in MAPK-interacting 
      enzymes. A docking domain in extracellular-signal-regulated kinase (ERK), a MAPK, 
      serves as a common site for binding to the MAPK kinase MEK1, the MAPK-activated 
      protein kinase MNK1 and the MAPK phosphatase MKP3. Two aspartic acids in this 
      domain are essential for docking, one of which is mutated in the sevenmaker 
      mutant of Drosophila ERK/Rolled. A corresponding domain in the MAPKs p38 and 
      JNK/SAPK also serves as a common docking site for their MEKs, MAPK-activated 
      protein kinases and MKPs. These docking interactions increase the efficiency of 
      the enzymatic reactions. These findings reveal a hitherto unidentified docking 
      motif in MAPKs that is used in common for recognition of their activators, 
      substrates and regulators.
FAU - Tanoue, T
AU  - Tanoue T
AD  - Department of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku, 
      Kyoto 606-8502, Japan.
FAU - Adachi, M
AU  - Adachi M
FAU - Moriguchi, T
AU  - Moriguchi T
FAU - Nishida, E
AU  - Nishida E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nat Cell Biol
JT  - Nature cell biology
JID - 100890575
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
RN  - EC 2.7.12.2 (MAP Kinase Kinase 1)
RN  - EC 2.7.12.2 (Map2k1 protein, mouse)
RN  - EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
RN  - EC 3.1.3.48 (Dual Specificity Phosphatase 6)
RN  - EC 3.1.3.48 (Dusp6 protein, mouse)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
SB  - IM
MH  - *Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism
MH  - *Conserved Sequence
MH  - Dual Specificity Phosphatase 6
MH  - MAP Kinase Kinase 1
MH  - Mitogen-Activated Protein Kinase 1/metabolism
MH  - Mitogen-Activated Protein Kinase Kinases/metabolism
MH  - Mitogen-Activated Protein Kinases/*metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Protein Serine-Threonine Kinases/metabolism
MH  - Protein Tyrosine Phosphatases/metabolism
MH  - p38 Mitogen-Activated Protein Kinases
EDAT- 2000/02/03 09:00
MHDA- 2000/03/25 09:00
CRDT- 2000/02/03 09:00
PHST- 2000/02/03 09:00 [pubmed]
PHST- 2000/03/25 09:00 [medline]
PHST- 2000/02/03 09:00 [entrez]
AID - 10.1038/35000065 [doi]
PST - ppublish
SO  - Nat Cell Biol. 2000 Feb;2(2):110-6. doi: 10.1038/35000065.