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Fidéline Bonnet-Serrano and Jérôme Bertherat

of the regulatory subunit of PKA, were identified at the 17q22–24 locus and are responsible for more than two-thirds of Carney complex index cases, from 37% in the sporadic forms to 80% in the typical familial forms ( Bertherat et al. 2009 ). The

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Graeme B Bolger, Mariana F Bizzi, Sergio V Pinheiro, Giampaolo Trivellin, Lisa Smoot, Mary-Ann Accavitti, Márta Korbonits, and Antonio Ribeiro-Oliveira Jr

al. 2007 , Francis et al. 2011 ). cAMP signaling pathways, working through spatially distinct subpopulations of the cAMP effectors, the cAMP-dependent protein kinase A (PKA) and the exchange protein activated by cAMP (Epac), differentially

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A Tsigginou, E Bimpaki, M Nesterova, A Horvath, S Boikos, C Lyssikatos, C Papageorgiou, C Dimitrakakis, A Rodolakis, C A Stratakis, and A Antsaklis

Introduction Protein kinase A (PKA), a serine–threonine kinase and the main effector of cAMP signaling in most cells, is widely involved in the regulation of cell growth and proliferation ( Robinson-White et al . 2006 a , b ). PKA holoenzyme is a

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Lawrence S Kirschner, Zhirong Yin, Georgette N Jones, and Emilia Mahoney

Introduction PKA as a pre-eminent second messenger system Protein kinase A (PKA) or the cAMP-dependent protein kinase is a serine–threonine kinase that was characterized initially as mediating the effects of elevated cAMP levels, which arose as a

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Stephanie Espiard, Ludivine Drougat, Nikolaos Settas, Sara Haydar, Kerstin Bathon, Edra London, Isaac Levy, Fabio R Faucz, Davide Calebiro, Jérôme Bertherat, Dong Li, Michael A Levine, and Constantine A Stratakis

Introduction Protein kinase A (PKA) is a tetrameric enzyme composed of a regulatory (R) subunit dimer and two catalytic (C) subunits. The R- and C- subunits disassociate when cAMP molecules bind to each R-subunit, releasing C-subunits to

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Kiran Nadella, Fabio R Faucz, and Constantine A Stratakis

Introduction Genetic defects in protein kinase A (PKA) regulatory subunit type 1A (PRKAR1A) lead to increased cyclic adenosine monophosphate (cAMP) signaling and primary pigmented nodular adrenocortical disease (PPNAD) associated with

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Hongyu Chen, Dan Liu, Zhengyan Yang, Limin Sun, Que Deng, Shuo Yang, Lu Qian, Liang Guo, Ming Yu, Meiru Hu, Ming Shi, and Ning Guo

cells expressing the Notch receptors and regulate tumor angiogenesis ( Zeng et al . 2005 , Li et al . 2007 ). In this study, we show that catecholamines upregulate the expression of Jagged 1 in breast cancer cells through the β2-AR–PKA–mTOR pathway

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Emmanouil Saloustros, Paraskevi Salpea, Matthew Starost, Sissi Liu, Fabio R Faucz, Edra London, Eva Szarek, Woo-Jin Song, Mehboob Hussain, and Constantine A Stratakis

A , which codes for the regulatory subunit type 1α (RIa) of the cAMP-dependent protein kinase A (PKA) and is located on chromosome 17q23–24 have been detected in approximately 70% of the kindreds with known CNC ( Kirschner et al . 2000 , Bertherat

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Arvind Thakkar, Ahmed Aljameeli, Shibu Thomas, and Girish V Shah

completely abolished by mPKI, a specific cell-permeable inhibitor of cAMP-dependent protein kinase (PKA; Sabbisetti et al . 2005 ). These results are consistent with the current evidence that PKA, along with Rho-family GTPases, plays a key role in the

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Inga Mertens-Walker, Christine Bolitho, Robert C Baxter, and Deborah J Marsh

cells ( Schiffenbauer et al . 2002 ). Furthermore, gonadotropins have been shown to promote invasion of ovarian cancer cells through the phosphatidylinositol 3-kinase (PI3K) and protein kinase A (PKA) pathways in SKOV-3 ovarian cancer cells ( Choi et