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My name is Susan Taylor.
I'm a professor of chemistry
and biochemistry and
also pharmacology at
the University of
California San Diego.
I'm also an investigator of
the Howard Hughes
Medical Institute.
I'd like to tell you
today about Protein,
Kinase, Structure,
Function and Regulation.
I'll talk about the entire
kinome which you see here,
as well as one specific member
of that protein
kinase superfamily.
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If we look more closely
at the human kinome,
I'd like to give you a
little perspective on
the whole field of protein
phosphorylation and
historically how this
family evolved In
our science over the
last half century.
It's one of the
largest gene families.
Little less than two percent
of the human genome codes for
protein kinases.
They're probably
five or six splice
variants for each.
So it's a very
large gene family.
The protein phosphorylation
story began in
the late 1950s with
the work of Ed Krebs
and Eddie Fisher,
who discovered for
phosphorylase kinase and
its ability to phosphorylate
and regulate glycogen
phosphorylase.
That was the first
protein kinase to be
discovered PKA cyclic
cAMP-dependent
protein kinase was the second.
That was about a decade later,
also by Ed Krebs and Don Walsh.
Then a third important part of
this family only became
apparent after another decade.
This was the finding that Src,
which was an oncogene,
was a protein kinase
when it was cloned.
You could tell from
the sequence it was
related to this superfamily.
Then the finding by
Eckardt Sefton and
Tony Hunter that Src
phosphorylated not Syrian and
threatening, but
Tyrosine residues.
It meant that this was
a very large family
of proteins that
phosphorylated serine,
threonine, and tyrosine.
We're going to focus in
particular on one
branch of this kinome,
the AGC kinase is
protein kinase AGC and one
particular member PKA.
