Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts Quantitative analysis of individual sites by solid-phase microsequencing
Por:
Arness B., Manjarrez-Hernandez H.A., Howell S.A., Learmonth M., Aitken A.
Publicada:
1 ene 1992
Resumen:
A synthetic peptide, KKKKRFSFKKSFKLSGFSFKK, containing the phosphorylation sites of the acidic 80-87 kDa protein kinase C substrate was used to identify phosphopeptides in enzyme digests of this protein from mouse fibroblast C3H/10T1/2 cells. Stimulation of phosphorylation occurred, in vivo, with TPA at Ser7, Ser11 and Ser18, and, will two less potent phorbol esters, at Ser7 and Ser18. Okadaic acid effected a net phosphorylation of Ser7 and/or Ser11. Solid-phase sequencing showed that, in vitro, the order of initial rate of phosphorylation was Ser11 > Ser7 > Ser18, while Ser18 was preferentially phosphorylated when either Ser7 or Ser11 was occupied. No significant phosphorylation of Ser15 was detected. © 1992.
Filiaciones:
Arness B.:
Laboratory of Protein Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom
Manjarrez-Hernandez H.A.:
Laboratory of Protein Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom
Howell S.A.:
Laboratory of Protein Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom
Learmonth M.:
Thrombosis Research Institute, Emmanuel Kaye Building, Manresa Road, London, SW3 6LR, United Kingdom
Aitken A.:
Laboratory of Protein Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom
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