Protein kinase structure, function and regulation

Published on November 30, 2010   45 min

A selection of talks on Biochemistry

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0:00
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.
0:28
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.

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Protein kinase structure, function and regulation

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