PMID- 10207045
OWN - NLM
STAT- MEDLINE
DCOM- 19990520
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 17
DP  - 1999 Apr 23
TI  - Dual specificity protein kinase activity of testis-specific protein kinase 1 and 
      its regulation by autophosphorylation of serine-215 within the activation loop.
PG  - 12171-6
AB  - TESK1 (testis-specific protein kinase 1) is a protein kinase with a structure
      composed of an N-terminal protein kinase domain and a C-terminal proline-rich
      domain. Whereas the 3.6-kilobase TESK1 mRNA is expressed predominantly in the
      testis, a faint 2.5-kilobase TESK1 mRNA is expressed ubiquitously. The kinase
      domain of TESK1 contains in the catalytic loop in subdomain VIB an unusual DLTSKN
      sequence, which is not related to the consensus sequence of either
      serine/threonine kinases or tyrosine kinases. In this study, we show that TESK1
      has kinase activity with dual specificity on both serine/threonine and tyrosine
      residues. In an in vitro kinase reaction, the kinase domain of TESK1 underwent
      autophosphorylation on serine and tyrosine residues and catalyzed phosphorylation
      of histone H3 and myelin basic protein on serine, threonine, and tyrosine
      residues. Site-directed mutagenesis analyses revealed that Ser-215 within the
      "activation loop" of the kinase domain is the site of serine autophosphorylation 
      of TESK1. Replacement of Ser-215 by alanine almost completely abolished serine
      autophosphorylation and histone H3 kinase activities. In contrast, replacement of
      Ser-215 by glutamic acid abolished serine autophosphorylation activity but
      retained histone H3 kinase activity. These results suggest that
      autophosphorylation of Ser-215 is an important step to positively regulate the
      kinase activity of TESK1.
FAU - Toshima, J
AU  - Toshima J
AD  - Department of Biology, Faculty of Science, Kyushu University, Hakozaki,
      Higashi-ku, Fukuoka 812-8581, Japan.
FAU - Tanaka, T
AU  - Tanaka T
FAU - Mizuno, K
AU  - Mizuno K
LA  - eng
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 (DNA Primers)
RN  - 3KX376GY7L (Glutamic Acid)
RN  - 452VLY9402 (Serine)
RN  - EC 2.7.1.- (testis-specific protein kinase 1)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - OF5P57N2ZX (Alanine)
SB  - IM
MH  - Alanine/chemistry/metabolism
MH  - Animals
MH  - Base Sequence
MH  - COS Cells
MH  - Catalytic Domain
MH  - DNA Primers
MH  - Enzyme Activation
MH  - Glutamic Acid/chemistry/metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Mutagenesis, Site-Directed
MH  - Phosphorylation
MH  - Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism
MH  - Rats
MH  - Serine/*metabolism
MH  - Substrate Specificity
EDAT- 1999/04/17 00:00
MHDA- 1999/04/17 00:01
CRDT- 1999/04/17 00:00
PHST- 1999/04/17 00:00 [pubmed]
PHST- 1999/04/17 00:01 [medline]
PHST- 1999/04/17 00:00 [entrez]
AID - 10.1074/jbc.274.17.12171 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 23;274(17):12171-6. doi: 10.1074/jbc.274.17.12171.