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Rapid and reversible translocation of the catalytic subunit of cAMP‐dependent protein kinase type II from the Golgi complex to the nucleus.
Author(s) -
Nigg E.A.,
Hilz H.,
Eppenberger H.M.,
Dutly F.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb04006.x
Subject(s) - biology , protein subunit , nucleus , golgi apparatus , protein kinase a , chromosomal translocation , microbiology and biotechnology , kinase , biochemistry , gene , endoplasmic reticulum
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.