Purification and characterisation of an insulin‐stimulated protein‐serine kinase which phosphorylates acetyl‐CoA carboxylase

FEBS Letters

Moule, S.K¹  Heesom, K.J¹  Denton, R.M¹ 

[1] Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, UK

关键词: Insulin;    Acetyl-CoA carboxylase;    Serine phosphorylation;    Protein activator;    Rat epididymal adipose tissue;   

DOI  :  10.1016/S0014-5793(97)01597-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An insulin-stimulated protein kinase specific for acetyl-CoA carboxylase has been purified from rat epididymal adipose tissue using Mono-Q chromatography. The kinase binds to (and phosphorylates) the relatively inactive, dimeric form of acetyl-CoA carboxylase, but not to its active, polymeric form, and this property has been used to purify the kinase. Under the conditions used, phosphorylation by the purified kinase did not result in a detectable increase in acetyl-CoA carboxylase activity. These studies also led to the recognition of an `activator' protein which is capable of increasing the activity of acetyl-CoA carboxylase without changing its phosphorylation state. It is suggested that this `activator' protein, together with the insulin-activated acetyl-CoA carboxylase kinase, may play a role in the activation of acetyl-CoA carboxylase by insulin.

【 授权许可】

Unknown