cAMP-PKA signal transduction specificity in Saccharomyces cerevisiae
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MINI-REVIEW
cAMP‑PKA signal transduction specificity in Saccharomyces cerevisiae P. Portela1 · Silvia Rossi1 Received: 23 August 2020 / Revised: 23 August 2020 / Accepted: 1 September 2020 © Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Living cells have developed a set of complex signaling responses, which allow them to withstand different environmental challenges. Signaling pathways enable the cell to monitor external and internal states and to articulate the appropriate physiological responses. Cellular signal transmission requires the dynamic formation of spatiotemporal controlled molecular interactions. One of the most important signaling circuits in Saccharomyces cerevisiae is the one controlled by cAMP-Protein Kinase A (PKA). In budding yeast, extracellular glucose and a plethora of signals related with growth and stress conditions regulate the intracellular cAMP levels that modulate PKA activity which in turn regulates a broad range of cellular processes. The cAMP-PKA signaling output requires a controlled specificity of the PKA responses. In this review we discuss the molecular mechanisms that are involved in the establishment of the specificity in the cAMP-PKA signaling pathway in S.cerevisiae. Keywords cAMP-PKA · Specificity · Signal transduction · Anchoring proteins · Bcy1 · TPK · Transcription-P-bodies · Stress granules · Saccharomyces cerevisiae
Introduction Cells sense extracellular stimuli to adjust intracellular processes appropriately to changes in the environment and to maintain cellular homeostasis. Therefore, the key is to ensure that the signals must be specific and subjected to strict control of the regulatory response (Li and Qian 2003; Hynes et al. 2013; Lee and Yaffe 2016). In most cases, cells respond to the environmental changes by signaling through the action of enzyme cascades. Spatial and temporal control of signal transduction is frequently achieved by compartmentalization of intracellular effectors through adaptors or anchoring proteins (Pawson and Scott 2010). In many cases, the signal recognized by a receptor triggers the synthesis of a second messenger which in turn controls the activity of kinases. These kinases phosphorylate their downstream substrates. A widely known example of a
Communicated by M. Kupiec. * Silvia Rossi [email protected] 1
Instituto de Química Biológica de La Facultad de Ciencias Exactas y Naturales (IQUIBICEN), CONICET-Universidad de Buenos Aires, Buenos Aires, Argentina
second messenger is cAMP, which activates cAMP-dependent protein kinase (PKA) (Taylor et al. 2005, 2013). PKA in Saccharomyces cerevisiae is a tetramer composed of two regulatory subunits and two catalytic subunits. The cAMP binding regulatory subunit is encoded by a single gene BCY1, while the catalytic subunits are encoded by the TPK1, TPK2 and TPK3 genes (Toda et al. 1987). In the absence of cAMP, the Bcy1 dimer binds two catalytic subunits (Tpk) and the enzyme is in the inactive state. The cAMP-PKA signaling in S.cereviciae (Thevelein et al. 2008; Con
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