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Purification and characterisation of an insulin‐stimulated protein‐serine kinase which phosphorylates acetyl‐CoA carboxylase
Author(s) -
Heesom K.J,
Moule S.K,
Denton R.M
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01597-4
Subject(s) - pyruvate carboxylase , acetyl coa carboxylase , biochemistry , activator (genetics) , phosphorylation , protein kinase a , kinase , chemistry , mitogen activated protein kinase kinase , biology , enzyme , gene
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.