The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The literature retrieved consistently links Ppk34 to Schizosaccharomyces pombe ORF SPCC1919.01 and identifies it as a CaMKK-family, serine/threonine protein kinase; in a Ca2+-signaling study it was renamed Ckk2 (for CaM kinase kinase 2). (cisnerosbarroso2014negativefeedbackregulation pages 8-9, cisnerosbarroso2014negativefeedbackregulation pages 13-14, cisnerosbarroso2014negativefeedbackregulation pages 10-12)
Cisneros-Barroso et al. report that SPCC1919.01/Ppk34 (Ckk2) is most similar to mammalian CaMKK2 and also related to the other fission-yeast CaMKK-like kinase Ssp1. (cisnerosbarroso2014negativefeedbackregulation pages 10-12)
CaMKKs (Ca2+/calmodulin-dependent protein kinase kinases) are upstream kinases that activate other protein kinases—classically CaMKs and AMPK—via phosphorylation of their activation loops. In S. pombe, at least two CaMKK-like kinases are discussed in the retrieved sources: Ssp1 and Ppk34/Ckk2. (davie2015nitrogenregulatesampk pages 1-2, davie2015nitrogenregulatesampk pages 7-8, cisnerosbarroso2014negativefeedbackregulation pages 10-12)
In fission yeast, the AMPK catalytic α subunit Ssp2 is activated by phosphorylation of its T-loop site Thr189, which then can inhibit TORC1 signaling under nutrient stress, affecting growth and mitotic commitment. (davie2015nitrogenregulatesampk pages 1-2, davie2015nitrogenregulatesampk pages 5-7, davie2015nitrogenregulatesampk pages 7-8)
Ppk34/Ckk2 is annotated as a serine/threonine protein kinase (EC 2.7.11.1) and is experimentally supported to function as an upstream kinase regulator (CaMKK-like), rather than only a dispensable “unknown” kinase. (bimbo2005systematicdeletionanalysis pages 2-3, cisnerosbarroso2014negativefeedbackregulation pages 13-14)
Limitations: In the retrieved primary sources, no direct in vitro kinase assay of purified Ppk34/Ckk2 (with kinetic parameters or direct substrate mapping) was captured; functional inference is therefore based on genetic requirements for downstream phosphorylation events and pathway phenotypes. (cisnerosbarroso2014negativefeedbackregulation pages 13-14, davie2015nitrogenregulatesampk pages 7-8)
A. Ca2+-stress signaling: Ckk2 → Cmk1
Cisneros-Barroso et al. identify Ckk2 (Ppk34/SPCC1919.01) as the kinase responsible for Cmk1 phosphorylation in response to Ca2+ stress. Loss of Ckk2 eliminates the Ca2+-induced Cmk1 phosphorylation mobility shift. (cisnerosbarroso2014negativefeedbackregulation pages 10-12)
B. Nitrogen-stress signaling: Ppk34 → AMPKα/Ssp2 Thr189 phosphorylation dynamics
Davie et al. show that nitrogen stress causes an increase in Ssp2 Thr189 phosphorylation (detected using a phospho-AMPK antibody cross-reactive due to activation-loop conservation) and that Ppk34 is specifically required for this stress-induced increase, while basal Thr189 phosphorylation is still present without Ppk34. (davie2015nitrogenregulatesampk pages 7-8)
Davie et al. demonstrate that nitrogen stress activates AMPK/Ssp2 and inhibits TORC1. The paper explicitly states that a second CaMKK homolog Ppk34 is specifically required to stimulate activation of Ssp2 in response to nitrogen stress, while Ssp1 is constitutively required for basal T-loop phosphorylation. (davie2015nitrogenregulatesampk pages 1-2, davie2015nitrogenregulatesampk pages 7-8)
Mechanistically, nitrogen stress led to an average 2.5-fold increase in Ssp2 Thr189 phosphorylation after 30 minutes, and this increase was absent in ppk34Δ cells. (davie2015nitrogenregulatesampk pages 7-8)
Functionally, ppk34Δ fails to accelerate mitosis and reduce cell size at division after nitrogen stress; importantly, rapamycin rescues this failure, supporting a model in which Ppk34 acts upstream of TORC1 inhibition during nitrogen stress. (davie2015nitrogenregulatesampk pages 7-8)
Davie et al. also note that nitrogen-stress-induced AMPK activation (mitotic acceleration) occurs independently of the AMPK β and γ subunits, implying an atypical regulation of the AMPK catalytic subunit in this system and motivating models in which Ppk34 contributes to α-subunit activation without canonical AMP-sensing inputs. (davie2015nitrogenregulatesampk pages 5-7)
Cisneros-Barroso et al. place Ckk2 upstream of Cmk1 in a Ca2+-triggered signaling module that counterbalances calcineurin signaling: calcineurin promotes Prz1 activation/nuclear localization, while Ckk2 activates Cmk1, and Cmk1 phosphorylates/inactivates Prz1 (promoting nuclear export), forming a negative feedback loop in Ca2+ signaling. (cisnerosbarroso2014negativefeedbackregulation pages 13-14)
Genetically, Δckk2 phenocopies Δcmk1 in Ca2+ resistance, and the Δcmk1 Δckk2 double mutant is also Ca2+-resistant, supporting that Ckk2 and Cmk1 act in the same pathway for Ca2+ signaling outputs. (cisnerosbarroso2014negativefeedbackregulation pages 10-12)
Additionally, Ckk2 is linked to the Cdc25 protein-level response under Ca2+ stress: Δckk2 cells show Cdc25 protein behavior similar to Δcmk1 and fail to increase Cdc25 during Ca2+ response in the cited time course. (cisnerosbarroso2014negativefeedbackregulation pages 10-12)
A kinase-deletion screen for NETO (new end take-off) regulators identified ppk34 deletion as associated with increased bipolar growth, leading to its classification as a putative negative regulator of NETO in that screen. (koyano2010searchforkinases pages 3-3)
Quantitatively, the polarity fractions reported for ppk34Δ were:
- 25°C: 39.8% monopolar, 47.1% bipolar, 13.1% septated
- 36°C: 31.9% monopolar, 55.9% bipolar, 12.2% septated (koyano2010searchforkinases pages 3-3)
No direct imaging-based localization (e.g., Ppk34-GFP) was captured in the retrieved excerpts. The Ca2+ signaling model described by Cisneros-Barroso et al. treats Ckk2/Cmk1 and calcineurin as cytosolic cascades that control the nuclear–cytoplasmic shuttling of Prz1, but this is a pathway-level inference rather than direct localization of Ckk2. (cisnerosbarroso2014negativefeedbackregulation pages 13-14, cisnerosbarroso2014negativefeedbackregulation pages 10-12)
A systematic kinase deletion analysis categorized Ppk34 (SPCC1919.01) deletion as viable and listed it as “unknown” with respect to process/function in their Table 1 annotation, indicating it is non-essential under standard conditions assayed in that work. (bimbo2005systematicdeletionanalysis pages 2-3)
Across later targeted/functional screens and mechanistic studies, ppk34Δ/ckk2Δ exhibits clear condition-dependent phenotypes:
- Defective nitrogen-stress AMPK activation and mitotic acceleration (rescued by rapamycin), consistent with impaired TORC1 inhibition in that context. (davie2015nitrogenregulatesampk pages 7-8)
- Altered Ca2+ signaling outputs, including Ca2+ resistance when Ckk2/Cmk1 negative feedback on Prz1 is removed. (cisnerosbarroso2014negativefeedbackregulation pages 10-12)
- Altered growth polarity (NETO) regulation with increased bipolarity in screen conditions. (koyano2010searchforkinases pages 3-3)
A 2023 review on AMPK–TOR interplay in yeast reiterates the central role of the Ssp1–Ssp2–TORC1 axis in environmental stress responses and mitotic advancement, highlighting that stresses including nitrogen deprivation lead to Ssp2-dependent TORC1 inhibition and premature mitotic entry. (alao2023interplaysofampk pages 6-8)
While the review emphasizes Ssp1/Ssp2 regulation and downstream TOR effects, it is consistent with the primary literature establishing stress-specific upstream contributions (including Ppk34 in nitrogen-stress activation) and underscores ongoing interest in how yeast tune distinct stress responses. (alao2023interplaysofampk pages 6-8)
Within the retrieved corpus, no 2023–2024 primary studies focusing directly on Ppk34/Ckk2 molecular mechanism, structure, or localization were identified. Therefore, the most experimentally specific functional assignments remain dominated by 2014–2015 mechanistic work and earlier genetic screens. (alao2023interplaysofampk pages 6-8)
| Aspect | Key finding | Evidence type | Experimental details/conditions | Quantitative data | Source (first author year journal) | DOI/URL |
|---|---|---|---|---|---|---|
| Identity | ORF SPCC1919.01, previously named Ppk34, was identified as a second CaMKK-family kinase in S. pombe and renamed Ckk2; it is most similar to mammalian CaMKK2 and also related to Ssp1. (cisnerosbarroso2014negativefeedbackregulation pages 8-9, cisnerosbarroso2014negativefeedbackregulation pages 13-14, cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Sequence comparison, genetic | BLAST/sequence comparison in Ca2+-signaling study; compared with human CaMKK1/2 and Ssp1. (cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Ckk2 similarity: 34% identity to human CaMKK2, 32% to Ssp1, 28% to human CaMKK1; coverages 86%, 63%, 52%, respectively. (cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Cisneros-Barroso 2014 Nucleic Acids Research | https://doi.org/10.1093/nar/gku684 |
| Molecular function | Ppk34/Ckk2 functions as an upstream serine/threonine kinase in a CaMKK-like role, activating downstream kinases in stress signaling rather than being merely an uncharacterized kinase. (cisnerosbarroso2014negativefeedbackregulation pages 13-14) | Genetic, biochemical inference | Ca2+ response assays and pathway analysis place Ckk2 upstream of Cmk1; nitrogen-stress assays place Ppk34 upstream of AMPK/Ssp2 activation. (davie2015nitrogenregulatesampk pages 7-8, cisnerosbarroso2014negativefeedbackregulation pages 13-14) | No direct catalytic constants reported for Ppk34/Ckk2 itself in retrieved sources. (davie2015nitrogenregulatesampk pages 7-8, cisnerosbarroso2014negativefeedbackregulation pages 13-14) | Cisneros-Barroso 2014 Nucleic Acids Research; Davie 2015 Current Biology | https://doi.org/10.1093/nar/gku684; https://doi.org/10.1016/j.cub.2014.12.034 |
| Substrates | In the Ca2+ pathway, Ckk2/Ppk34 is required for Cmk1 phosphorylation/activation; in the nitrogen-stress pathway, Ppk34 is required for the increase in AMPKα/Ssp2 Thr189 phosphorylation. (cisnerosbarroso2014negativefeedbackregulation pages 13-14, davie2015nitrogenregulatesampk pages 7-8) | Biochemical, genetic | For Cmk1: CaCl2 treatment and mobility-shift assays in wt vs Δckk2. For Ssp2: glutamate→proline shift, western blot with anti-phospho-AMPK antibody in wt vs ppk34Δ. (davie2015nitrogenregulatesampk pages 7-8, cisnerosbarroso2014negativefeedbackregulation pages 10-12) | AMPK/Ssp2 Thr189 phosphorylation increased ~2.5-fold after 30 min nitrogen stress in wt; this increase was absent in ppk34Δ. (davie2015nitrogenregulatesampk pages 7-8) | Davie 2015 Current Biology; Cisneros-Barroso 2014 Nucleic Acids Research | https://doi.org/10.1016/j.cub.2014.12.034; https://doi.org/10.1093/nar/gku684 |
| Pathways | Ppk34/Ckk2 participates in at least two distinct signaling modules: Ckk2→Cmk1→Prz1/Cdc25 in Ca2+ signaling and Ppk34→Ssp2/AMPK→TORC1 inhibition during nitrogen stress. (davie2015nitrogenregulatesampk pages 1-2, cisnerosbarroso2014negativefeedbackregulation pages 13-14) | Genetic, biochemical, review | Ca2+ stress: 100 mM CaCl2 time courses and mutant analysis. Nitrogen stress: shift from glutamate to proline and TORC1 readouts/Maf1 phosphorylation/rapamycin rescue. Review literature summarizes this axis in yeast physiology. (davie2015nitrogenregulatesampk pages 5-7, davie2015nitrogenregulatesampk pages 7-8, alao2023interplaysofampk pages 6-8) | Nitrogen stress activates Ssp2 and inhibits TORC1; rapamycin rescues the ppk34Δ mitotic-entry defect. (davie2015nitrogenregulatesampk pages 7-8) | Davie 2015 Current Biology; Cisneros-Barroso 2014 Nucleic Acids Research; Alao 2023 Cells | https://doi.org/10.1016/j.cub.2014.12.034; https://doi.org/10.1093/nar/gku684; https://doi.org/10.3390/cells12040519 |
| Localization | Retrieved primary papers support cytosolic signaling function for the Ckk2/Cmk1/Prz1 module but do not provide a direct subcellular localization experiment for Ppk34/Ckk2 itself. (cisnerosbarroso2014negativefeedbackregulation pages 13-14, cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Inference from pathway model | Model places calcineurin, Ckk2, and Cmk1 as Ca2+-responsive cytosolic cascades acting on Prz1 nuclear shuttling; no direct GFP-localization of Ckk2 reported in retrieved excerpts. (cisnerosbarroso2014negativefeedbackregulation pages 13-14, cisnerosbarroso2014negativefeedbackregulation pages 10-12) | No direct localization percentages or compartment-enrichment values reported. (cisnerosbarroso2014negativefeedbackregulation pages 13-14, cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Cisneros-Barroso 2014 Nucleic Acids Research | https://doi.org/10.1093/nar/gku684 |
| Phenotypes | ppk34Δ/ckk2Δ is viable and was initially unassigned functionally in the systematic kinase-deletion set, but later screens and mechanistic work linked it to polarity and stress signaling. (bimbo2005systematicdeletionanalysis pages 2-3, koyano2010searchforkinases pages 3-3, cisnerosbarroso2014negativefeedbackregulation pages 13-14) | Deletion screen, genetic | Genome-wide kinase deletion study; NETO/polarity screen; Ca2+ sensitivity and nitrogen-stress mitotic-entry assays. (bimbo2005systematicdeletionanalysis pages 2-3, koyano2010searchforkinases pages 3-3, davie2015nitrogenregulatesampk pages 7-8) | Among 106 kinases analyzed, 17 essential and 89 dispensable; Ppk34 was among viable deletions. (bimbo2005systematicdeletionanalysis pages 2-3) | Bimbó 2005 Eukaryotic Cell; Koyano 2010 Bioscience, Biotechnology, and Biochemistry; Cisneros-Barroso 2014 Nucleic Acids Research | https://doi.org/10.1128/ec.4.4.799-813.2005; https://doi.org/10.1271/bbb.100223; https://doi.org/10.1093/nar/gku684 |
| Phenotypes | In a growth-polarity screen, ppk34 deletion increased bipolar growth, identifying Ppk34 as a putative negative regulator of NETO. (koyano2010searchforkinases pages 3-3, koyano2010searchforkinases pages 1-3) | Genetic screen | Quantified monopolar/bipolar/septated cells at 25°C and 36°C in kinase-deletion strains. (koyano2010searchforkinases pages 3-3, koyano2010searchforkinases pages 1-3) | 25°C: 39.8% monopolar, 47.1% bipolar, 13.1% septated; 36°C: 31.9% monopolar, 55.9% bipolar, 12.2% septated. (koyano2010searchforkinases pages 3-3) | Koyano 2010 Bioscience, Biotechnology, and Biochemistry | https://doi.org/10.1271/bbb.100223 |
| Phenotypes | In Ca2+ stress, Δckk2 and Δcmk1 Δckk2 are Ca2+-resistant, similar to Δcmk1, supporting that Ckk2 and Cmk1 act in the same pathway. (cisnerosbarroso2014negativefeedbackregulation pages 13-14, cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Genetic | Spot assays on YES plates containing CaCl2; comparison of wt, Δcmk1, Δckk2, and double mutant. (cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Resistance phenotype observed on plates with 50–75 mM CaCl2 and with 100 mM CaCl2 in signaling assays. (cisnerosbarroso2014negativefeedbackregulation pages 9-10, cisnerosbarroso2014negativefeedbackregulation pages 10-12) | Cisneros-Barroso 2014 Nucleic Acids Research | https://doi.org/10.1093/nar/gku684 |
| Phenotypes | In nitrogen stress, ppk34Δ fails to accelerate mitosis and does not reduce cell size at division to the same extent as wild type; rapamycin rescues this defect, placing Ppk34 upstream of TORC1. (davie2015nitrogenregulatesampk pages 7-8) | Genetic, pharmacological | Early exponential cultures shifted from glutamate to proline; mutants analyzed for mitotic-entry timing and response to rapamycin. (davie2015nitrogenregulatesampk pages 7-8) | Qualitative rescue by rapamycin reported; no exact rescue percentage given in retrieved excerpt. (davie2015nitrogenregulatesampk pages 7-8) | Davie 2015 Current Biology | https://doi.org/10.1016/j.cub.2014.12.034 |
| Quantitative stats | Ppk34 specifically controls stress-induced AMPK activation, whereas Ssp1 is required for basal Ssp2 Thr189 phosphorylation; thus the two CaMKK-like kinases show nonredundant specificity. (davie2015nitrogenregulatesampk pages 7-8, alao2023interplaysofampk pages 6-8) | Biochemical, genetic, review | wt, ssp1Δ, and ppk34Δ compared under steady-state and nitrogen-stress conditions; phospho-specific westerns and Phos-tag gels used. (davie2015nitrogenregulatesampk pages 7-8) | ppk34Δ: basal Thr189 phosphorylation retained, but no stress-induced increase; ssp1Δ: Thr189 phosphorylation absent even basally. (davie2015nitrogenregulatesampk pages 7-8) | Davie 2015 Current Biology; Alao 2023 Cells | https://doi.org/10.1016/j.cub.2014.12.034; https://doi.org/10.3390/cells12040519 |
| Quantitative stats | AMPK activation by nitrogen stress in S. pombe can occur without the AMPK β and γ subunits, highlighting an unusual activation mode in which Ppk34 contributes to α-subunit activation. (davie2015nitrogenregulatesampk pages 1-2, davie2015nitrogenregulatesampk pages 5-7, alao2023interplaysofampk pages 6-8) | Biochemical, genetic, review | amk2Δ, cbs2Δ, and double mutants assayed after glutamate→proline shift; Ssp2 T189 phosphorylation and mitotic response monitored. (davie2015nitrogenregulatesampk pages 5-7, alao2023interplaysofampk pages 6-8) | β/γ subunits not essential for mitotic advancement under nitrogen stress; wt Ssp2 T189 phosphorylation rises ~2.5-fold after 30 min. (davie2015nitrogenregulatesampk pages 7-8) | Davie 2015 Current Biology; Alao 2023 Cells | https://doi.org/10.1016/j.cub.2014.12.034; https://doi.org/10.3390/cells12040519 |
| Current understanding / gap | Recent authoritative review literature continues to place S. pombe Ppk34/Ckk2 within the AMPK–TOR stress-response network, but 2023–2024 primary literature specifically focused on Ppk34/Ckk2 is sparse in the retrieved corpus. (alao2023interplaysofampk pages 6-8) | Review / literature-gap assessment | 2023 review summarizes Ssp1/Ssp2/TOR cross-talk and cites earlier work showing ppk34-related nitrogen-stress signaling. (alao2023interplaysofampk pages 6-8) | No new 2023–2024 Ppk34-specific quantitative primary dataset identified in retrieved sources. (alao2023interplaysofampk pages 6-8) | Alao 2023 Cells | https://doi.org/10.3390/cells12040519 |
Table: This table compiles the main experimentally supported findings for S. pombe Ppk34/Ckk2 (Q9UU87/SPCC1919.01), including identity, pathway placement, phenotypes, and quantitative results. It highlights where direct evidence exists and where current knowledge remains inferential or limited.
Primary supported function: Ppk34 (Ckk2) is a CaMKK-family Ser/Thr kinase that mediates stress-responsive activation of downstream kinases.
- In nitrogen stress, it is required for the stress-induced increase in AMPKα/Ssp2 activation-loop phosphorylation (Thr189), enabling efficient TORC1 inhibition and mitotic advancement under poor nitrogen. (davie2015nitrogenregulatesampk pages 7-8)
- In Ca2+ stress, it functions upstream of Cmk1 to regulate a negative-feedback loop opposing calcineurin-dependent activation of Prz1, with downstream impacts on Cdc25 dynamics and Ca2+ tolerance phenotypes. (cisnerosbarroso2014negativefeedbackregulation pages 10-12)
Localization: Not directly resolved in the retrieved literature excerpts; pathway logic suggests a cytosolic kinase acting on signaling components controlling nuclear shuttling of transcription factors, but direct tagging/localization remains a key evidence gap. (cisnerosbarroso2014negativefeedbackregulation pages 13-14)
References
(cisnerosbarroso2014negativefeedbackregulation pages 8-9): Eugenia Cisneros-Barroso, Tula Yance-Chávez, Ayako Kito, Reiko Sugiura, Alba Gómez-Hierro, David Giménez-Zaragoza, and Rosa Aligue. Negative feedback regulation of calcineurin-dependent prz1 transcription factor by the camkk-camk1 axis in fission yeast. Nucleic Acids Research, 42:9573-9587, Jul 2014. URL: https://doi.org/10.1093/nar/gku684, doi:10.1093/nar/gku684. This article has 20 citations and is from a highest quality peer-reviewed journal.
(cisnerosbarroso2014negativefeedbackregulation pages 13-14): Eugenia Cisneros-Barroso, Tula Yance-Chávez, Ayako Kito, Reiko Sugiura, Alba Gómez-Hierro, David Giménez-Zaragoza, and Rosa Aligue. Negative feedback regulation of calcineurin-dependent prz1 transcription factor by the camkk-camk1 axis in fission yeast. Nucleic Acids Research, 42:9573-9587, Jul 2014. URL: https://doi.org/10.1093/nar/gku684, doi:10.1093/nar/gku684. This article has 20 citations and is from a highest quality peer-reviewed journal.
(cisnerosbarroso2014negativefeedbackregulation pages 10-12): Eugenia Cisneros-Barroso, Tula Yance-Chávez, Ayako Kito, Reiko Sugiura, Alba Gómez-Hierro, David Giménez-Zaragoza, and Rosa Aligue. Negative feedback regulation of calcineurin-dependent prz1 transcription factor by the camkk-camk1 axis in fission yeast. Nucleic Acids Research, 42:9573-9587, Jul 2014. URL: https://doi.org/10.1093/nar/gku684, doi:10.1093/nar/gku684. This article has 20 citations and is from a highest quality peer-reviewed journal.
(davie2015nitrogenregulatesampk pages 1-2): Elizabeth Davie, Gabriella M.A. Forte, and Janni Petersen. Nitrogen regulates ampk to control torc1 signaling. Current Biology, 25:445-454, Feb 2015. URL: https://doi.org/10.1016/j.cub.2014.12.034, doi:10.1016/j.cub.2014.12.034. This article has 107 citations and is from a highest quality peer-reviewed journal.
(davie2015nitrogenregulatesampk pages 7-8): Elizabeth Davie, Gabriella M.A. Forte, and Janni Petersen. Nitrogen regulates ampk to control torc1 signaling. Current Biology, 25:445-454, Feb 2015. URL: https://doi.org/10.1016/j.cub.2014.12.034, doi:10.1016/j.cub.2014.12.034. This article has 107 citations and is from a highest quality peer-reviewed journal.
(davie2015nitrogenregulatesampk pages 5-7): Elizabeth Davie, Gabriella M.A. Forte, and Janni Petersen. Nitrogen regulates ampk to control torc1 signaling. Current Biology, 25:445-454, Feb 2015. URL: https://doi.org/10.1016/j.cub.2014.12.034, doi:10.1016/j.cub.2014.12.034. This article has 107 citations and is from a highest quality peer-reviewed journal.
(bimbo2005systematicdeletionanalysis pages 2-3): Andrea Bimbó, Yonghui Jia, Siew Lay Poh, R. Krishna Murthy Karuturi, Nicole den Elzen, Xu Peng, Liling Zheng, Matthew O'Connell, Edison T. Liu, Mohan K. Balasubramanian, and Jianhua Liu. Systematic deletion analysis of fission yeast protein kinases. Eukaryotic Cell, 4:799-813, Apr 2005. URL: https://doi.org/10.1128/ec.4.4.799-813.2005, doi:10.1128/ec.4.4.799-813.2005. This article has 124 citations and is from a peer-reviewed journal.
(koyano2010searchforkinases pages 3-3): Takayuki KOYANO, Kazunori KUME, Manabu KONISHI, Takashi TODA, and Dai HIRATA. Search for kinases related to transition of growth polarity in fission yeast. Bioscience, Biotechnology, and Biochemistry, 74:1129-1133, May 2010. URL: https://doi.org/10.1271/bbb.100223, doi:10.1271/bbb.100223. This article has 35 citations.
(alao2023interplaysofampk pages 6-8): John-Patrick Alao, Luc Legon, Aleksandra Dabrowska, Anne-Marie Tricolici, Juhi Kumar, and Charalampos Rallis. Interplays of ampk and tor in autophagy regulation in yeast. Cells, 12:519, Feb 2023. URL: https://doi.org/10.3390/cells12040519, doi:10.3390/cells12040519. This article has 33 citations.
(koyano2010searchforkinases pages 1-3): Takayuki KOYANO, Kazunori KUME, Manabu KONISHI, Takashi TODA, and Dai HIRATA. Search for kinases related to transition of growth polarity in fission yeast. Bioscience, Biotechnology, and Biochemistry, 74:1129-1133, May 2010. URL: https://doi.org/10.1271/bbb.100223, doi:10.1271/bbb.100223. This article has 35 citations.
(cisnerosbarroso2014negativefeedbackregulation pages 9-10): Eugenia Cisneros-Barroso, Tula Yance-Chávez, Ayako Kito, Reiko Sugiura, Alba Gómez-Hierro, David Giménez-Zaragoza, and Rosa Aligue. Negative feedback regulation of calcineurin-dependent prz1 transcription factor by the camkk-camk1 axis in fission yeast. Nucleic Acids Research, 42:9573-9587, Jul 2014. URL: https://doi.org/10.1093/nar/gku684, doi:10.1093/nar/gku684. This article has 20 citations and is from a highest quality peer-reviewed journal.