PMID- 10497253
OWN - NLM
STAT- MEDLINE
DCOM- 19991102
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 40
DP  - 1999 Oct 1
TI  - Isolation of the protein kinase TAO2 and identification of its mitogen-activated 
      protein kinase/extracellular signal-regulated kinase kinase binding domain.
PG  - 28803-7
AB  - We previously reported the cloning of the thousand and one-amino acid protein
      kinase 1 (TAO1), a rat homolog of the Saccharomyces cerevisiae protein kinase
      sterile 20 protein. Here we report the complete sequence and properties of a
      related rat protein kinase TAO2. Like TAO1, recombinant TAO2 selectively
      activated mitogen-activated protein/extracellular signal-regulated kinase kinases
      (MEKs) 3, 4, and 6 of the stress-responsive mitogen-activated protein kinase
      pathways in vitro and copurified with MEK3 endogenous to Sf9 cells. To examine
      TAO2 interactions with MEKs, the MEK binding domain of TAO2 was localized to an
      approximately 135-residue sequence just C-terminal to the TAO2 catalytic domain. 
      In vitro this MEK binding domain associated with MEKs 3 and 6 but not MEKs 1, 2, 
      or 4. Using chimeric MEK proteins, we found that the MEK N terminus was
      sufficient for binding to TAO2. Catalytic activity of full-length TAO2 enhanced
      its binding to MEKs. However, neither the autophosphorylation of the MEK binding 
      domain of TAO2 nor the activity of MEK itself was required for MEK binding. These
      results suggest that TAO proteins lie in stress-sensitive kinase cascades and
      define a mechanism by which these kinases may organize downstream targets.
FAU - Chen, Z
AU  - Chen Z
AD  - Department of Pharmacology, University of Texas Southwestern Medical Center,
      Dallas, Texas 75235-9041, USA.
FAU - Hutchison, M
AU  - Hutchison M
FAU - Cobb, M H
AU  - Cobb MH
LA  - eng
SI  - GENBANK/AF140556
GR  - GM53032/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (TAO2 protein, rat)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 2.7.11.25 (MAP Kinase Kinase Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Calcium-Calmodulin-Dependent Protein Kinases/*metabolism
MH  - Cell Line
MH  - DNA, Complementary
MH  - MAP Kinase Kinase Kinases/genetics/*isolation & purification/metabolism
MH  - Molecular Sequence Data
MH  - Protein-Serine-Threonine Kinases
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Spodoptera
EDAT- 1999/09/25 00:00
MHDA- 1999/09/25 00:01
CRDT- 1999/09/25 00:00
PHST- 1999/09/25 00:00 [pubmed]
PHST- 1999/09/25 00:01 [medline]
PHST- 1999/09/25 00:00 [entrez]
AID - 10.1074/jbc.274.40.28803 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 1;274(40):28803-7. doi: 10.1074/jbc.274.40.28803.