The PKA regulatory subunit from yeast forms a homotetramer: Low-resolution structure of the N-terminal oligomerization domain

Bardeci, Nicolás Diego González; Caramelo, Julio J.; Blumenthal, Donald K.; Rinaldi, Jimena; Rossi, Silvia; Moreno, Sílvia

doi:10.1016/j.jsb.2015.12.001

Cited by 9 publications

(6 citation statements)

References 64 publications

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“…In mammalian cells, the D/D domain is required for the dimerization of the regulatory subunits, and the interaction exposes a hydrophobic groove that serves as a binding platform for AKAPs (Banky et al, 2003). A bioinformatic analysis of sequences from 99 fungi revealed the existence of the canonical D/D domain (1–50 amino acids) in 63 species distributed across four phyla and one subphylum; the 36 fungal sequences lacking the predicted N-terminal region domain belong to the pezizomycotina subphylum (González Bardeci et al, 2016). This study also characterized the structure of Bcy1 and identified a novel tetrameric form leading to a model in which the protein consists of a dimer of dimers via oligomerization of the D/D domain.…”

Section: Mechanisms Of Nutrient Sensing Mediated By the Camp/pka Pathmentioning

confidence: 99%

“…This study also characterized the structure of Bcy1 and identified a novel tetrameric form leading to a model in which the protein consists of a dimer of dimers via oligomerization of the D/D domain. This organization putatively creates two classical AKAP binding surfaces and additional sites for electrostatic interactions, and suggests that tetramerization of regulatory subunits may allow interaction with a wide range of intracellular partners including AKAPs (González Bardeci et al, 2016) (Figure 1).…”

Section: Mechanisms Of Nutrient Sensing Mediated By the Camp/pka Pathmentioning

confidence: 99%

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The cAMP/Protein Kinase A Pathway Regulates Virulence and Adaptation to Host Conditions in Cryptococcus neoformans

Caza

Kronstad

2019

Front. Cell. Infect. Microbiol.

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Nutrient sensing is critical for adaptation of fungi to environmental and host conditions. The conserved cAMP/PKA signaling pathway contributes to adaptation by sensing the availability of key nutrients such as glucose and directing changes in gene expression and metabolism. Interestingly, the cAMP/PKA pathway in fungal pathogens also influences the expression of virulence determinants in response to nutritional and host signals. For instance, protein kinase A (PKA) in the human pathogen Cryptococcus neoformans plays a central role in orchestrating phenotypic changes, such as capsule elaboration and melanin production, that directly impact disease development. In this review, we focus first on insights into the role of the cAMP/PKA pathway in nutrient sensing for the model yeast Saccharomyces cerevisiae to provide a foundation for understanding the pathway in C. neoformans . We then discuss key features of cAMP/PKA signaling in C. neoformans including new insights emerging from the analysis of transcriptional and proteomic changes in strains with altered PKA activity and expression. Finally, we highlight recent studies that connect the cAMP/PKA pathway to cell surface remodeling and the formation of titan cells.

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Section: Mechanisms Of Nutrient Sensing Mediated By the Camp/pka Pathmentioning

confidence: 99%

Section: Mechanisms Of Nutrient Sensing Mediated By the Camp/pka Pathmentioning

confidence: 99%

The cAMP/Protein Kinase A Pathway Regulates Virulence and Adaptation to Host Conditions in Cryptococcus neoformans

Caza

Kronstad

2019

Front. Cell. Infect. Microbiol.

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“…Translocation is thought to bring PKA in closer proximity to its substrates, which sensitizes the kinase to cAMP, allowing the catalytic subunit to phosphorylate substrate proteins. Structural and sequence analysis of yeast Bcy1 revealed that the N-terminal region responsible for dimerization and for docking to AKAPs (D/D domain) in higher eukaryotic R1 subunits is not well conserved in yeast (63). Bcy1 also lacks the two redox sensor cysteine residues that are oxidized by hydrogen peroxide in mammalian cells and regulation via AKAP interaction remains ill-defined in fungi (64).…”

Section: Discussionmentioning

confidence: 99%

Tolerance to nascent protein misfolding stress requires fine-tuning of the cAMP/PKA pathway

Kritsiligkou

Nowicki-Osuch

Carter

et al. 2021

Journal of Biological Chemistry

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“…Bcy1 localisation is variable and responsive to environmental and nutritional conditions [116,136]. Bcy1 N-terminus structure is similar to the canonical mammal RIIα domain (DD domain) as it has a helixturn-helix motif and the critical amino acids for dimerization [137,138]. However, the binding domain of proteins described as Bcy1 interactors in S. cerevisiae displays different molecular features than the canonical domain of their mammalian counterparts, AKAPs (A-Kinase Anchoring Proteins, DD-AKAP), which contain essential hydrophobic residues [139][140][141].…”

Section: Pka Anchoring Through Bcy1 Interacting Proteinsmentioning

confidence: 99%

The cAMP-PKA signalling crosstalks with CWI and HOG-MAPK pathways in yeast cell response to osmotic and thermal stress

Galello,

Bermúdez-Moretti,

Ortolá Martínez

et al. 2024

Microb Cell

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The yeast Saccharomyces cerevisiae is widely used in food and non-food industries. During industrial fermentation yeast strains are exposed to fluctuations in oxygen concentration, osmot-ic pressure, pH, ethanol concentration, nutrient availability and temperature. Fermentation performance depends on the ability of the yeast strains to adapt to these changes. Suboptimal conditions trigger responses to the external stimuli to allow homeostasis to be maintained. Stress-specific signalling pathways are activated to co-ordinate changes in transcription, translation, protein function, and metabolic fluxes while a transient arrest of growth and cell cycle progression occur. cAMP-PKA, HOG-MAPK and CWI signalling path-ways are turned on during stress response. Comprehension of the mechanisms involved in the responses and in the adaptation to these stresses during fermentation is key to improving this industri-al process. The scope of this review is to outline the advancement of knowledge about the cAMP-PKA signalling and the crosstalk of this pathway with the CWI and HOG-MAPK cascades in response to the environmental challenges heat and hyperosmotic stress.

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The PKA regulatory subunit from yeast forms a homotetramer: Low-resolution structure of the N-terminal oligomerization domain

Cited by 9 publications

References 64 publications

The cAMP/Protein Kinase A Pathway Regulates Virulence and Adaptation to Host Conditions in Cryptococcus neoformans

The cAMP/Protein Kinase A Pathway Regulates Virulence and Adaptation to Host Conditions in Cryptococcus neoformans

Tolerance to nascent protein misfolding stress requires fine-tuning of the cAMP/PKA pathway

The cAMP-PKA signalling crosstalks with CWI and HOG-MAPK pathways in yeast cell response to osmotic and thermal stress

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