Thr94 in bovine myelin basic protein is a second phosphorylation site for 42-kDa mitogen-activated protein kinase (ERK2).
作者： Daniel Hirschberg , Olof Rådmark , Hans Jörnvall , Tomas Bergman
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摘要: Treatment of bovine brain myelin basic protein with 42-kDa mitogen-activated kinase [p42 MAPK or extracellular signal-regulated 2 (ERK2)] in the presence ATP and Mg2+ results phosphorylation Thr94 Thr97. is not previously known to be an ERK2 site. Both residues are phosphorylated about same extent highly conserved segment Asn91-Ile-Val-Thr94-Pro-Arg-Thr97-Pro-Pro-Pro-Ser101 MALDI mass spectrometry before after treatment revealed addition two phosphate groups protein. Tryptic cleavage resulted a single fragment (positions 91-104) carrying observed increase. Tandem applied tryptic peptide showed that both Thr97 acceptors phosphate. A singly species could detected. Identification site reveals nontraditional acceptor position, preceded by three noncharged (Asn-Ile-Val). Proline at position -2 -3 from site, typical for recognition sequence proline-directed kinases, missing. The provide information delineation further substrate consensus motif phosphorylation.
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