Differential localization to cytoplasm, nucleus or P-bodies of yeast PKA subunits under different growth conditions

Tudisca, Vanesa Romina; Recouvreux, Victoria; Moreno, Silvia N.J.; Boy‐Marcotte, Emmanuelle; Jacquet, Michel; Portela, Paula

doi:10.1016/j.ejcb.2009.08.005

Cited by 71 publications

(102 citation statements)

References 40 publications

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“…Moreover, our results follow patterns of compartmentalized activation and inactivation (Fig. 3C), overlapping with previous results showing condition-dependent localization of yeast PKA subunits (28). Localizations with a stronger score than expected by chance are outlined (solid black line: P < 0.05; dotted line: P < 0.1) were 1, extracellular region; 2, cell wall; 3, plasma membrane; 4, Golgi apparatus; 5, peroxisome; 6, ribosome; 7, endoplasmic reticulum; 8, mitochondrial envelope; 9, mitochondrion; 10, cytoskeleton; 11, vacuole; 12, cellular bud; 13, vesicle; 14, nucleus; 15, nucleolus; 16, cytoplasm (not to scale).…”

Section: Resultssupporting

confidence: 92%

Systematic identification of signal integration by protein kinase A

Filteau

Diss

Torres-Quiroz

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Cellular processes and homeostasis control in eukaryotic cells is achieved by the action of regulatory proteins such as protein kinase A (PKA). Although the outbound signals from PKA directed to processes such as metabolism, growth, and aging have been well charted, what regulates this conserved regulator remains to be systematically identified to understand how it coordinates biological processes. Using a yeast PKA reporter assay, we identified genes that influence PKA activity by measuring proteinprotein interactions between the regulatory and the two catalytic subunits of the PKA complex in 3,726 yeast genetic-deletion backgrounds grown on two carbon sources. Overall, nearly 500 genes were found to be connected directly or indirectly to PKA regulation, including 80 core regulators, denoting a wide diversity of signals regulating PKA, within and beyond the described upstream linear pathways. PKA regulators span multiple processes, including the antagonistic autophagy and methionine biosynthesis pathways. Our results converge toward mechanisms of PKA posttranslational regulation by lysine acetylation, which is conserved between yeast and humans and that, we show, regulates protein complex formation in mammals and carbohydrate storage and aging in yeast. Taken together, these results show that the extent of PKA input matches with its output, because this kinase receives information from upstream and downstream processes, and highlight how biological processes are interconnected and coordinated by PKA.Ras/cAMP/PKA pathway | acetylation | methionine | autophagy | TOR

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Section: Resultssupporting

confidence: 92%

Systematic identification of signal integration by protein kinase A

Filteau

Diss

Torres-Quiroz

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…This result was expected for Tpk3 as this PKA subunit had been found previously to associate with P-body foci (Tudisca et al 2010). In contrast, this localization had not been observed for any of the other three enzymes.…”

Section: Protein Kinase Foci Defined Eight Different Stationary-phasesupporting

confidence: 74%

“…The remainder of this report is focused on these 17 enzymes. Tpk3, a catalytic subunit of the cAMP-dependent protein kinase, was also included in the subsequent analysis because it had been shown previously to be present in P-body foci (Tudisca et al 2010).…”

Section: Resultsmentioning

confidence: 99%

“…Four additional protein kinases were found to be present in both P-bodies and stress granules. Only one of these enzymes, the Tpk3 subunit of PKA, was known previously to be associated with these RNP granules (Tudisca et al 2010). The presence of these enzymes suggests that they might target specific proteins within these granules, and it will be important to determine whether they influence either the assembly or disassembly of these different structures.…”

Section: Discussionmentioning

confidence: 99%

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Protein Kinases Are Associated with Multiple, Distinct Cytoplasmic Granules in Quiescent Yeast Cells

Shah¹,

Nostramo²,

Zhang³

et al. 2014

Genetics

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The cytoplasm of the eukaryotic cell is subdivided into distinct functional domains by the presence of a variety of membrane-bound organelles. The remaining aqueous space may be further partitioned by the regulated assembly of discrete ribonucleoprotein (RNP) complexes that contain particular proteins and messenger RNAs. These RNP granules are conserved structures whose importance is highlighted by studies linking them to human disorders like amyotrophic lateral sclerosis. However, relatively little is known about the diversity, composition, and physiological roles of these cytoplasmic structures. To begin to address these issues, we examined the cytoplasmic granules formed by a key set of signaling molecules, the protein kinases of the budding yeast Saccharomyces cerevisiae. Interestingly, a significant fraction of these proteins, almost 20%, was recruited to cytoplasmic foci specifically as cells entered into the G 0 -like quiescent state, stationary phase. Colocalization studies demonstrated that these foci corresponded to eight different granules, including four that had not been reported previously. All of these granules were found to rapidly disassemble upon the resumption of growth, and the presence of each was correlated with cell viability in the quiescent cultures. Finally, this work also identified new constituents of known RNP granules, including the well-characterized processing body and stress granule. The composition of these latter structures is therefore more varied than previously thought and could be an indicator of additional biological activities being associated with these complexes. Altogether, these observations indicate that quiescent yeast cells contain multiple distinct cytoplasmic granules that may make important contributions to their long-term survival.

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“…We found that Kog1, a TORC1 subunit, moves from the vacuolar membrane to P-bodies. Interestingly, P-bodies have been previously shown to colocalize with other signaling molecules, including the PKA subunits Tpk2 and Tpk3 in SP (34). We observed that the presence of Kog1 in P-bodies was clearly reduced in hsp31Δ, strongly supporting that TORC1 is not properly regulated upon the deletion of Hsp31 minifamily genes.…”

Section: Discussionsupporting

confidence: 54%

Yeast DJ-1 superfamily members are required for diauxic-shift reprogramming and cell survival in stationary phase

Miller-Fleming

Antas

Pais

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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The yeast Hsp31 minifamily proteins (Hsp31, Hsp32, Hsp33, Hsp34) belong to the highly conserved DJ-1 superfamily. The human DJ-1 protein is associated with cancer and neurodegenerative disorders, such as Parkinson disease. However, the precise function of human and yeast DJ-1 proteins is unclear. Here we show that the yeast DJ-1 homologs have a role in diauxic-shift (DS), characterized by metabolic reprogramming because of glucose limitation. We find that the Hsp31 genes are strongly induced in DS and in stationary phase (SP), and that deletion of these genes reduces chronological lifespan, impairs transcriptional reprogramming at DS, and impairs the acquisition of several typical characteristics of SP, including autophagy induction. In addition, under carbon starvation, the HSP31 family gene-deletion strains display impaired autophagy, disrupted target of rapamycin complex 1 (TORC1) localization to P-bodies, and caused abnormal TORC1-mediated Atg13 phosphorylation. Repression of TORC1 by rapamycin in the gene-deletion strains completely reversed their sensitivity to heat shock. Taken together, our data indicate that Hsp31 minifamily is required for DS reprogramming and cell survival in SP, and plays a role upstream of TORC1. The enhanced understanding of the cellular function of these genes sheds light into the biological role of other members of the superfamily, including DJ-1, which is an attractive target for therapeutic intervention in cancer and in Parkinson disease.

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Differential localization to cytoplasm, nucleus or P-bodies of yeast PKA subunits under different growth conditions

Cited by 71 publications

References 40 publications

Systematic identification of signal integration by protein kinase A

Systematic identification of signal integration by protein kinase A

Protein Kinases Are Associated with Multiple, Distinct Cytoplasmic Granules in Quiescent Yeast Cells

Yeast DJ-1 superfamily members are required for diauxic-shift reprogramming and cell survival in stationary phase

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