C2 can do it, too.
In this issue of Cell, report that the C2 domain of the serine/threonine protein kinase Cdelta is a phosphotyrosine binding domain and present the crystal structure of this C2 domain bound to a peptide containing phosphotyrosine. Prior to this work, C2 domains were thought to bind only to phospholipids or to unphosphorylated proteins, and the SH2 and PTB domains were the only signaling domains known to recognize phosphotyrosine. This new role for the C2 domain links phosphotyrosine recognition directly to serine/threonine kinase activity and reveals an unexpected mechanism for crosstalk between distinct signaling pathways.
Sondermann
Holger
H
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, Berkeley, California 94720, USA.
Kuriyan
John
J
D000818:Animals; D006801:Humans; D011493:Protein Kinase C / Q000737:chemistry* / Q000378:metabolism*; D051745:Protein Kinase C-delta; D015398:Signal Transduction / Q000502:physiology*; D018909:src Homology Domains / Q000502:physiology*
C497258:PRKCD protein, human; D011493:Protein Kinase C; D051745:Protein Kinase C-delta