Phosphorylation and activation of p40 tyrosine kinase by casein kinase‐1

FEBS Letters

Itarte, Emilio²  Harrison, Marietta L.¹  Payne, D.Michael³  Weber, Michael J.³  Vila, Jordi⁴  Zioncheck, Thomas F.¹ 

[1] Department of Medicinal Chemistry and Pharmacognosy, School of Pharmacy, Purdue University, West Lafayette. IN 47907, USA;Departament Bioquimica i Biologia Molecular, Univ. Autonoma de Barcelona, Barcelona, Spain;Department of Microbiology and Cancer Center, Box 441, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA;Departement de Microbiologia, Hospital Clinic i Provincial de Barcelona, Facultat de Medicina, Villaroel 132, Barcelona 08036, Spain

关键词: Protein kinase;    Phosphotyrosine;    Casein kinase-1;    Protein;   

DOI  :  10.1016/0014-5793(90)80754-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Because examination of regulatory trans-phosphorylations can help elucidate the cellular functions of tyrosyi protein kinases, we have investigated the effects of phosphorylation by casein kinase-1 on the activity of the p40 tyrosyi protein kinase. We find that casein kinase-1 can phosphorylate the p40 tyrosyl kinase on serine and threonine residues, in part on a unique tryptic peptide. The phosphorylation induces a substantial increase in the tyrosyl protein kinase activity of p40, in contrast to most instances in which serine/threonine phosphorylation inhibits activity of tyrosyl protein kinases. These findings raise the possibility that p40 might be part of a protein phosphorylation network in which casein kinase-1 participates.

【 授权许可】

Unknown