TY - JOUR
T1 - The RIIβ regulatory subunit of protein kinase A binds to cAMP response element
T2 - An alternative cAMP signaling pathway
AU - Srivastava, Rakesh K.
AU - Lee, Youl Nam
AU - Noguchi, Kohei
AU - Park, Yun Gyu
AU - Ellis, Matthew J.C.
AU - Jeong, Jin Sook
AU - Kim, Se Nyun
AU - Cho-Chung, Yoon S.
PY - 1998/6/9
Y1 - 1998/6/9
N2 - cAMP, through the activation of cAMP-dependent protein kinase (PKA), is involved in transcriptional regulation. In eukaryotic cells, cAMP is not considered to alter the binding affinity of CREB/ATF to cAMP-responsive element (CRE) but to induce serine phosphorylation and consequent increase in transcriptional activity. In contrast, in prokaryotic cells, cAMP enhances the DNA binding of the catabolite repressor protein to regulate the transcription of several operons. The structural similarity of the CAMP binding sites in catabolite repressor protein and regulatory subunit of PKA type II (RH) suggested the possibility of a similar role for RII in eukaryotic gene regulation. Herein we report that RIIβ subunit of PKA is a transcription factor capable of interacting physically and functionally with a CRE. In contrast to CREB/ATF, the binding of RIIβ to a CRE was enhanced by cAMP, and in addition, RIIβ exhibited transcriptional activity as a Gal4- RIIβ fusion protein. These experiments identify RIIβ as a component of an alternative pathway for regulation of CRE-directed transcription in eukaryotic cells.
AB - cAMP, through the activation of cAMP-dependent protein kinase (PKA), is involved in transcriptional regulation. In eukaryotic cells, cAMP is not considered to alter the binding affinity of CREB/ATF to cAMP-responsive element (CRE) but to induce serine phosphorylation and consequent increase in transcriptional activity. In contrast, in prokaryotic cells, cAMP enhances the DNA binding of the catabolite repressor protein to regulate the transcription of several operons. The structural similarity of the CAMP binding sites in catabolite repressor protein and regulatory subunit of PKA type II (RH) suggested the possibility of a similar role for RII in eukaryotic gene regulation. Herein we report that RIIβ subunit of PKA is a transcription factor capable of interacting physically and functionally with a CRE. In contrast to CREB/ATF, the binding of RIIβ to a CRE was enhanced by cAMP, and in addition, RIIβ exhibited transcriptional activity as a Gal4- RIIβ fusion protein. These experiments identify RIIβ as a component of an alternative pathway for regulation of CRE-directed transcription in eukaryotic cells.
UR - http://www.scopus.com/inward/record.url?scp=0032499543&partnerID=8YFLogxK
U2 - 10.1073/pnas.95.12.6687
DO - 10.1073/pnas.95.12.6687
M3 - Article
C2 - 9618473
AN - SCOPUS:0032499543
SN - 0027-8424
VL - 95
SP - 6687
EP - 6692
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 12
ER -