Promiscuous subunit interactions: A possible mechanism for the regulation of protein kinase CK2
Author
dc.contributor.author
Allende, C. C.
Author
dc.contributor.author
Allende, J. E.
Admission date
dc.date.accessioned
2019-01-29T17:16:05Z
Available date
dc.date.available
2019-01-29T17:16:05Z
Publication date
dc.date.issued
1998
Identifier
dc.identifier.issn
07302312
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/163402
Abstract
dc.description.abstract
Protein kinase CK2 is a ubiquitous eukaryotic ser/thr protein kinase. The active holoenzyme is a heterotetrameric protein corn posed of catalytic (α and α') and regulatory (β) subunits that phosphorylates many different protein substrates and appears to be involved in the regulation of cell division. Despite important structural studies, the intimate details of the interactions of the α catalytic subunits with the β regulatory subunits are unknown. Recent evidence that indicates that both CK2 subunits can interact promiscuously with other proteins in a manner that excludes the binding of their complementary CK2 partners has opened the possibility that the phosphorylating activity of this enzyme may be regulated in a novel way. These alternative interactions could limit the in vivo availability of CK2 subunits to generate fully active holoenzyme CK2 tetramers. Likewise, variations in the ratio of α- and β-subunits could determine the activity of several phosphorylating and dephosphoryla