Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus.
AUTOR(ES)
Nigg, E A
RESUMO
In unstimulated interphase bovine epithelial (MDBK) cells, both regulatory (R II) and catalytic (C) subunits of the type II enzyme of cAMP-dependent protein kinase (cAMP-dPK II) are associated with the Golgi complex. However, as demonstrated by indirect immunofluorescence microscopy, within 5 min after stimulation of adenylate cyclase by forskolin, the C subunit dissociates from the Golgi-associated R II and becomes diffusely distributed. With increasing time of forskolin treatment, C subunits accumulate in the nucleus, while R II subunits remain associated with the Golgi complex. The effect of forskolin is rapidly reversible in that C subunits begin to reassociate with the Golgi complex within a few minutes after drug removal. C subunit translocations similar to those produced by forskolin also occur after treatment of MDBK cells with dibutyryl-cAMP, confirming that the observed effects are most likely mediated by elevation of intracellular cAMP levels. These results suggest that nuclear translocation of activated protein kinase subunits may represent an important link between hormonal stimuli and physiological responses.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=554581Documentos Relacionados
- Ethanol causes translocation of cAMP-dependent protein kinase catalytic subunit to the nucleus.
- Primary structure of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle.
- A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha.
- Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase.
- On the question of translocation of heart cAMP-dependent protein kinase.