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(Received for publication, January 22, 1996, and in revised form, August 1, 1996)
From the The A126 cell line, in contrast to its PC12
parent, does not differentiate, accumulate nuclear
cAMP-dependent protein kinase A (PKA) catalytic subunit, or
transcribe cAMP-dependent promoters in response to cAMP.
Total PKA is reduced by 50% and is partly resistant to cAMP-induced
dissociation in vivo. Unlike PC12, where PKAII is
membrane-associated, PKAII is exclusively cytosolic in A126.
Cotransfection with the RII anchor protein (AKAP75) and the PKA
catalytic subunit (C-PKA) restored cAMP-induced transcription to levels
found in PC12. These data indicate that membrane-bound PKAII amplifies
cAMP signaling to the nucleus and suggest that cAMP-mediated responses
are specified by the type and cellular localization of the PKA
isoform.
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29870-29875
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
,¶
Centro di Endocrinologia ed Oncologia
Sperimentale del CNR, c/o Dipartimento di Biologia e Patologia
Molecolare e Cellulare, Facoltà di Medicina, Università
"Federico II" 80131 Napoli, Italy, the § Institute of
Cancer Research, Columbia University, New York, New York 10032, and the
¶ Dipartimento di Medicina Sperimentale, Facoltà di Medicina
a Catanzaro, Università di Reggio Calabria, 88100 Catanzaro,
Italy
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