Abstract
The αβ heterodimeric form of untreated hepatic insulin receptor was a substrate for casein kinase 2, whereas the α2β2 heterotetramer was not. On the contrary, autophosphorylation was detected only in the heterotetramer. Dissociation of the receptor by treatment with dithiothreitol decreased its autophosphorylation but favoured phosphorylation of its β-subunit by casein kinase 2. © 1991.
Original language | English |
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Pages (from-to) | 15-18 |
Journal | FEBS Letters |
Volume | 283 |
Issue number | 1 |
DOIs | |
Publication status | Published - 20 May 1991 |
Keywords
- Casein kinase 2
- Insulin receptor
- Protein phosphorylation
- Rat liver