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J Biol Chem, Vol. 273, Issue 21, 12952-12959, May 22, 1998
,,,
From the After receiving an external stimulus
Dictyostelium amoebae are able to rearrange their actin
cytoskeleton within seconds, and phosphorylation is a prime candidate
for quick modification of cytoskeletal components. We isolated a kinase
from cytosolic extracts that specifically phosphorylated severin, a
Ca2+-dependent F-actin fragmenting protein. In
gel filtration chromatography severin kinase eluted with a molecular
mass of about 300 kDa and contained a 62-kDa component whose
autophosphorylation caused a mobility shift in SDS-polyacrylamide gel
electrophoresis and stimulated phosphorylation of severin. Severin
kinase activity could be specifically precipitated with antibodies
raised against the 62-kDa polypeptide. Phosphorylation of severin was
strongly reduced in the presence of Ca2+, indicating
additional regulation at the substrate level. Peptide sequencing and
cloning of the cDNA demonstrated that the 62-kDa protein belongs to
the Ste20p- or p21-activated protein kinase family. It is most closely
related to the germinal center kinase subfamily with its N-terminal
positioned catalytic domain followed by a presumptive regulatory domain
at the C terminus. The presence of a Ste20-like severin kinase in
Dictyostelium suggests a direct signal transduction from
the plasma membrane to the cytoskeleton by phosphorylation of
actin-binding proteins.
Adolf-Butenandt-Institut/Zellbiologie,
Ludwig-Maximilians-Universität, Schillerstrasse 42, 80336 München, Germany and the § Max-Planck-Institut
für Biochemie, Am Klopferspitz 18a,
82152 Martinsried, Germany
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