PMID- 10391943
OWN - NLM
STAT- MEDLINE
DCOM- 19990805
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 28
DP  - 1999 Jul 9
TI  - Molecular cloning and characterization of a novel dual specificity phosphatase,
      MKP-5.
PG  - 19949-56
AB  - A group of dual specificity protein phosphatases negatively regulates members of 
      the mitogen-activated protein kinase (MAPK) superfamily, which consists of three 
      major subfamilies, MAPK/extracellular signal-regulated kinase (ERK),
      stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK), and p38.
      Nine members of this group of dual specificity phosphatases have previously been 
      cloned. They show distinct substrate specificities for MAPKs, different tissue
      distribution and subcellular localization, and different modes of inducibility of
      their expression by extracellular stimuli. Here we have cloned and characterized 
      a novel dual specificity phosphatase, which we have designated MKP-5. MKP-5 is a 
      protein of 482 amino acids with a calculated molecular mass of 52.6 kDa and
      consists of 150 N-terminal amino acids of unknown function, two Cdc25 homology 2 
      regions in the middle, and a C-terminal catalytic domain. MKP-5 binds to p38 and 
      SAPK/JNK, but not to MAPK/ERK, and inactivates p38 and SAPK/JNK, but not
      MAPK/ERK. p38 is a preferred substrate. The subcellular localization of MKP-5 is 
      unique; it is present evenly in both the cytoplasm and the nucleus. MKP-5 mRNA is
      widely expressed in various tissues and organs, and its expression in cultured
      cells is elevated by stress stimuli. These results suggest that MKP-5 is a novel 
      type of dual specificity phosphatase specific for p38 and SAPK/JNK.
FAU - Tanoue, T
AU  - Tanoue T
AD  - Department of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku,
      Kyoto 606-8502, Japan.
FAU - Moriguchi, T
AU  - Moriguchi T
FAU - Nishida, E
AU  - Nishida E
LA  - eng
SI  - GENBANK/AB026436
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - 0 (ras-GRF1)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
RN  - EC 3.1.3.16 (DUSP10 protein, human)
RN  - EC 3.1.3.16 (Mitogen-Activated Protein Kinase Phosphatases)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
RN  - EC 3.1.3.48 (Dual-Specificity Phosphatases)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism
MH  - Cell Cycle Proteins/chemistry
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Dual-Specificity Phosphatases
MH  - Gene Expression Regulation, Enzymologic
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - JNK Mitogen-Activated Protein Kinases
MH  - Liver/enzymology
MH  - Mitogen-Activated Protein Kinase Phosphatases
MH  - *Mitogen-Activated Protein Kinases
MH  - Molecular Sequence Data
MH  - Phosphoprotein Phosphatases/chemistry/*genetics
MH  - Phosphorylation
MH  - Protein Binding
MH  - Protein Tyrosine Phosphatases/chemistry/*genetics
MH  - RNA, Messenger/metabolism
MH  - Recombinant Proteins/genetics
MH  - Sequence Alignment
MH  - Substrate Specificity
MH  - Transfection
MH  - Yeasts/genetics
MH  - p38 Mitogen-Activated Protein Kinases
MH  - ras-GRF1
EDAT- 1999/07/03 00:00
MHDA- 1999/07/03 00:01
CRDT- 1999/07/03 00:00
PHST- 1999/07/03 00:00 [pubmed]
PHST- 1999/07/03 00:01 [medline]
PHST- 1999/07/03 00:00 [entrez]
AID - 10.1074/jbc.274.28.19949 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 9;274(28):19949-56. doi: 10.1074/jbc.274.28.19949.