PMID- 10601328
OWN - NLM
STAT- MEDLINE
DCOM- 20000111
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 147
IP  - 6
DP  - 1999 Dec 13
TI  - A novel regulatory mechanism of MAP kinases activation and nuclear translocation 
      mediated by PKA and the PTP-SL tyrosine phosphatase.
PG  - 1129-36
AB  - Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP)
      kinases in the cytoplasm in an inactive form by association through a kinase
      interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine
      phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein
      kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the
      Ser(231) residue, located within the KIM. Upon phosphorylation of Ser(231),
      PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular
      signal-regulated kinase (ERK)1/2 and p38alpha were impaired. Furthermore,
      treatment of COS-7 cells with PKA activators, or overexpression of the Calpha
      catalytic subunit of PKA, inhibited the cytoplasmic retention of ERK2 and
      p38alpha by wild-type PTP-SL, but not by a PTP-SL S231A mutant. These findings
      support the existence of a novel mechanism by which PKA may regulate the
      activation and translocation to the nucleus of MAP kinases.
FAU - Blanco-Aparicio, C
AU  - Blanco-Aparicio C
AD  - Instituto de Investigaciones Citologicas, 46010 Valencia, Spain.
FAU - Torres, J
AU  - Torres J
FAU - Pulido, R
AU  - Pulido R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 17885-08-4 (Phosphoserine)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
RN  - EC 3.1.3.48 (PTPN5 protein, human)
RN  - EC 3.1.3.48 (PTPRR protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases, Non-Receptor)
RN  - EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 7)
SB  - IM
MH  - Amino Acid Motifs
MH  - Animals
MH  - Biological Transport
MH  - COS Cells
MH  - Cell Line
MH  - Cell Nucleus/*enzymology/*metabolism
MH  - Cyclic AMP-Dependent Protein Kinases/antagonists &
      inhibitors/chemistry/genetics/*metabolism
MH  - Cytoplasm/enzymology/metabolism
MH  - Enzyme Activation
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Mitogen-Activated Protein Kinase 1/genetics/metabolism
MH  - Mitogen-Activated Protein Kinase 3
MH  - Mitogen-Activated Protein Kinases/genetics/*metabolism
MH  - Models, Biological
MH  - Mutation/genetics
MH  - Nerve Tissue Proteins/chemistry/genetics/*metabolism
MH  - Phosphorylation
MH  - Phosphoserine/metabolism
MH  - Protein Tyrosine Phosphatases/chemistry/genetics/*metabolism
MH  - Protein Tyrosine Phosphatases, Non-Receptor
MH  - Receptor-Like Protein Tyrosine Phosphatases, Class 7
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Signal Transduction
MH  - Transfection
MH  - p38 Mitogen-Activated Protein Kinases
PMC - PMC2168101
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1083/jcb.147.6.1129 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Dec 13;147(6):1129-36. doi: 10.1083/jcb.147.6.1129.