Dissociation of the hepatic insulin receptor favours its phosphorylation by casein kinase 2

Ramon Trujillo; Marta Jose; Maria Plana; Elena Molina; Emilio Itarte

doi:10.1016/0014-5793(91)80543-C

Dissociation of the hepatic insulin receptor favours its phosphorylation by casein kinase 2

Ramon Trujillo, Marta Jose, Maria Plana, Elena Molina, Emilio Itarte

Research output: Contribution to journal › Article › Research › peer-review

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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
Pages (from-to)	15-18
Journal	FEBS Letters
Volume	283
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(91)80543-C
Publication status	Published - 20 May 1991

Keywords

Casein kinase 2
Insulin receptor
Protein phosphorylation
Rat liver

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Trujillo, R., Jose, M., Plana, M., Molina, E., & Itarte, E. (1991). Dissociation of the hepatic insulin receptor favours its phosphorylation by casein kinase 2. FEBS Letters, 283(1), 15-18. https://doi.org/10.1016/0014-5793(91)80543-C

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AU - Itarte, Emilio

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