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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target is correctly identified as Vas2/Aps1, ORF SPAP27G11.06c, UniProt Q9P7N2, from Schizosaccharomyces pombe strain 972. Exact-organism literature identifies vas2+/aps1+ as encoding the sigma small subunit of adaptor-protein complex 1 (AP-1). Thus, Vas2 is not an enzyme or transporter: its primary function is best understood as a noncatalytic structural/adaptor component of the AP-1 vesicle-coat machinery, acting in selective membrane-protein sorting and carrier formation around the trans-Golgi network (TGN), endosomes, and post-Golgi pathway. Direct Vas2 evidence is nevertheless sparse: its AP-1 identity and valproic-acid-sensitive phenotype are established, whereas detailed localization, cargo, secretion, and calcineurin conclusions rely mainly on experiments involving another S. pombe AP-1 subunit, Apm1. (zhang2013genomewidescreeningfor pages 1-2, zhang2013genomewidescreeningfor pages 2-3)
The supplied identity is internally consistent:
The exact S. pombe literature directly states that vas2+/aps1+ encodes the sigma subunit of AP-1, validating the supplied description. The family/domain combination is also appropriate for a small adaptin rather than a catalytic protein. (zhang2013genomewidescreeningfor pages 1-2)
The symbol is hazardous when searched without accession or ORF. Arabidopsis VAS2/GH3.17 is an unrelated auxin-metabolism protein. In addition, recent literature mentions an S. pombe protein called Aps1 with Nudix-type inositol-pyrophosphatase/polyphosphatase activity; that protein is not evidence that Q9P7N2 is an enzyme. These homonyms must be excluded by requiring the combined identifiers Q9P7N2 + SPAP27G11.06c + AP-1 sigma subunit. (koc2026speciescontextreverses pages 31-32)
AP complexes are heteromeric cytosolic adaptors that are recruited to selected membranes, recognize sorting information in cargo proteins, and connect cargo selection to coated-carrier formation. AP-1 is principally associated with TGN/endosomal trafficking. In S. pombe, the AP-1 μ1 subunit Apm1 was experimentally linked to trans-Golgi protein sorting, abnormal post-Golgi vesicle formation when deleted, and selective cargo-trafficking defects. (kita2004lossofapm1 pages 4-5, kita2004lossofapm1 pages 1-2, kita2004lossofapm1 pages 2-3)
Within this architecture, Vas2 is the small sigma subunit. Its likely role is to stabilize the AP-1 core and help create the conformational/structural platform through which the complex associates with membranes and cargo. The supplied AP1_sigma and AP_complex_ssu domains, together with the longin-like-domain assignment, strongly support this structural role. There is no basis to assign Vas2 a catalytic reaction, enzyme substrate, or transported solute.
The most defensible primary annotation is therefore:
Vas2 is a nonenzymatic small adaptin that functions as an integral structural subunit of the clathrin-associated AP-1 complex, supporting selective sorting and vesicular transport of membrane cargo at the TGN–endosome/post-Golgi interface.
A qualification is essential: direct Vas2-binding partners, cargo-recognition residues, membrane-recruitment kinetics, and a Vas2-containing complex structure have not been demonstrated in the retrieved S. pombe literature. Recognition of YXX-type sorting signals is discussed for AP adaptor machinery, but it should not be attributed specifically to Vas2 without a direct biochemical or structural experiment. (kita2004lossofapm1 pages 2-3)
No direct Vas2 fluorescent-localization experiment was retrieved. Localization is consequently inferred from verified AP-1 membership and direct observations of the S. pombe AP-1 μ1 subunit.
Apm1-GFP localized to Golgi/endosomal puncta, as assessed in part using the membrane/endocytic tracer FM4-64 after five minutes. Apm1 was additionally observed at the medial region and spindle-pole body and interacted with Sad1, but these latter localizations should not automatically be assigned to Vas2. (kita2004lossofapm1 pages 8-9, kita2004lossofapm1 pages 11-12)
Loss of Apm1 produced swollen or enlarged Golgi stacks, abnormal Golgi-associated membranes, and putative post-Golgi secretory-vesicle accumulation. Approximately 10% of mutant cells displayed abnormal structures under permissive conditions, and accumulated large vesicles were about 100–150 nm in diameter; the defects increased after temperature elevation or calcineurin inhibition. These data place the Apm1-containing AP-1 machinery at the Golgi/endosomal and post-Golgi trafficking interface. (kita2004lossofapm1 pages 4-5)
Accordingly, Vas2 most likely performs its function on the cytosolic face of TGN/Golgi and endosomal membranes during AP-1 coat assembly and cargo sorting. It is not predicted to be secreted, lumenal, or an integral membrane protein.
In apm1 mutants, the exocytic SNARE Syb1 failed to reach polarized secretion sites and accumulated in Golgi/endosomal compartments. Acid-phosphatase reporter secretion was reduced at 27°C and abolished after transfer to 36°C or exposure to FK506. These findings support an AP-1 requirement for efficient post-Golgi secretion and polarized cargo delivery. They are direct evidence for the pathway containing Apm1, not proof that Syb1 binds Vas2. (kita2004lossofapm1 pages 8-9, kita2004lossofapm1 pages 4-5, kita2004lossofapm1 pages 1-2)
The defect was selective rather than a complete block in endocytosis: Lucifer-yellow uptake showed no detectable delay over 30 minutes. AP-1 therefore appears to control particular sorting and recycling routes rather than bulk fluid-phase internalization. (kita2004lossofapm1 pages 8-9)
A 2012 study found that the GPI-anchored proteins Ecm33 and Gaz2 depended on an Apm1-associated, clathrin-mediated post-Golgi route for efficient surface delivery. In apm1-deletion cells, GFP-Ecm33 and GFP-Gaz2 accumulated in intracellular puncta rather than reaching their normal surface/medial distributions. Ecm33-positive structures colocalized with FM4-64 and the Golgi/endosome marker Krp1-RFP. Again, this identifies cargoes affected by disruption of another AP-1 subunit; direct cargo–Vas2 contact was not shown. Publication: July 2012, DOI/URL: https://doi.org/10.1371/journal.pone.0041946. (jaiseng2012studiesonthe pages 7-8)
Apm1 loss caused cell-wall-integrity, cytokinesis, and vacuole-fusion defects. Osmotic stabilization with 1.2 M sorbitol rescued temperature-associated growth and cytokinesis defects but not FK506 sensitivity, indicating that compromised cell integrity explains part—but not all—of the phenotype. These broad outcomes are most plausibly downstream consequences of defective trafficking of proteins and membrane material rather than separate enzymatic functions of AP-1. (kita2004lossofapm1 pages 8-9, kita2004lossofapm1 pages 11-12)
The clearest gene-specific phenotype is valproic-acid (VPA) hypersensitivity. Vas2/Aps1 was identified among previously isolated VPA-sensitive, membrane-trafficking-defective mutants, and the 2013 study explicitly connected the gene to the AP-1 sigma subunit. Publication: July 2013, DOI/URL: https://doi.org/10.1371/journal.pone.0068738. (zhang2013genomewidescreeningfor pages 5-7, zhang2013genomewidescreeningfor pages 1-2)
The genome-wide screen provides useful scale:
These data establish Vas2 as relevant to VPA tolerance, but they do not demonstrate that VPA binds Vas2 or directly inhibits AP-1. The authors’ broader interpretation is that defective trafficking sensitizes cells to VPA-associated cellular and cell-wall stress. VPA also elicited effects distinguishable from those of another aliphatic-acid HDAC inhibitor, including increased cytoplasmic Ca²⁺ through the Cch1–Yam8 channel, so the drug phenotype is probably multifactorial. (zhang2013genomewidescreeningfor pages 5-7, zhang2013genomewidescreeningfor pages 1-2)
The strongest signaling connection is with calcineurin, a Ca²⁺/calmodulin-dependent phosphatase that promotes fungal stress tolerance. In S. pombe, apm1 deletion caused FK506 hypersensitivity, and no viable apm1/calcineurin-deletion double mutant was recovered, indicating synthetic lethality or an exceptionally strong genetic interaction. Calcineurin inhibition intensified Golgi/vesicle, secretion, cytokinesis, and integrity defects. This supports partially overlapping roles for AP-1-dependent trafficking and calcineurin-mediated stress adaptation, but no direct Vas2–calcineurin interaction or dephosphorylation event was demonstrated. (kita2004lossofapm1 pages 4-5, kita2004lossofapm1 pages 1-2, kita2004lossofapm1 pages 2-3)
Apm1-associated phenotypes also implicated Ypt3-dependent exocytic/Rab trafficking: apm1 cells resembled ypt3 mutants in cell-wall integrity and were hypersensitive to dominant-negative Ypt3. This is pathway-level evidence involving Apm1; it does not establish direct Vas2–Ypt3 binding. (kita2004lossofapm1 pages 11-12)
No 2023–2024 paper directly characterizing Q9P7N2/SPAP27G11.06c Vas2 was identified. Consequently, the latest exact-gene mechanistic evidence in the retrieved corpus remains older genetics, particularly the 2013 VPA screen.
The most relevant recent development is a January 2024 study in the pathogenic yeast Candida glabrata, not S. pombe. A genome-wide FK506 screen identified 87 calcineurin-dependent fitness genes; more than 79% were linked to vesicular trafficking, and 69 were predicted to affect trafficking or ER functions. Hits included AP-1/AP-1R components, and targeted aps1Δ, apl2Δ, and arf1Δ mutants were strongly hypersensitive to calcineurin inhibitors. The study interpreted AP-1 as participating in clathrin- and Arf1-dependent Golgi-to-endosome trafficking whose disruption increases reliance on calcineurin. Publication: January 2024, DOI/URL: https://doi.org/10.1128/msphere.00554-23. These results strengthen the evolutionary plausibility of an AP-1–calcineurin stress-buffering relationship but cannot be transferred directly to S. pombe Vas2. (pavesic2024calcineurindependentcontributionsto pages 2-6)
A broader 2023 synthesis similarly emphasized calcineurin-dependent compensation for vesicular-trafficking defects across fungi, but the retrieved item was not a peer-reviewed Vas2 study and provides only comparative context. (pavesic2023regulationofcellular pages 53-62, pavesic2023regulationofcellular pages 19-23)
There is no evidence that Vas2 itself has a current clinical, diagnostic, agricultural, or industrial implementation. Its practical value is as a research-system component:
| Claim/topic | Conclusion | Evidence type | Key quantitative details | Confidence/limitations |
|---|---|---|---|---|
| Target identity | vas2/aps1 (SPAP27G11.06c; UniProt Q9P7N2) in Schizosaccharomyces pombe encodes the sigma small subunit of adaptor-protein complex 1 (AP-1). Exact organism and accession must anchor identification. (zhang2013genomewidescreeningfor pages 1-2) | Direct vas2 evidence; supplied UniProt/domain annotation | The 2013 study explicitly identifies vas2+/aps1+ as encoding the AP-1 sigma subunit. | High. Exact-symbol, organism-specific literature agrees with the supplied accession, description, family, and domains. |
| Molecular role | Vas2 is best annotated as a nonenzymatic structural/adaptor component of heterotetrameric AP-1, helping form the adaptor core used for cargo selection and clathrin-associated membrane-carrier formation; no catalytic reaction or substrate is expected. | Supplied UniProt/domain annotation; AP-1 family inference | Domains supplied for Q9P7N2 include AP1_sigma, AP_complex_ssu, AP_mu_sigma_su, longin-like-domain superfamily, and Clat_adaptor_s. | High for structural membership; moderate for exact molecular contacts. No Vas2-specific structure, binding assay, or cargo-recognition measurement was found. |
| Cellular localization | Vas2 most likely acts on Golgi/endosomal and post-Golgi membranes, but this is principally a complex-level inference. In S. pombe, Apm1-GFP localizes to Golgi/endosomal puncta, while loss of Apm1 produces abnormal Golgi-associated and post-Golgi vesicular structures. (kita2004lossofapm1 pages 8-9, kita2004lossofapm1 pages 4-5, kita2004lossofapm1 pages 1-2) | Direct other AP-1 subunit/whole-complex evidence | FM4-64 colocalization was assessed after 5 min; abnormal structures occurred in about 10% of apm1 cells at permissive temperature; accumulated vesicles were approximately 100–150 nm. | Moderate for Vas2. Strong evidence for the Apm1-containing AP-1 pathway, but no direct Vas2 fluorescent-localization experiment was retrieved. Apm1 additionally localizes to the medial region and spindle-pole body, which should not automatically be assigned to Vas2. |
| Trafficking direction and process | The best-supported pathway is AP-1-dependent sorting/carrier formation at the trans-Golgi network–endosome/post-Golgi interface, supporting secretion, recycling, and delivery of selected membrane proteins rather than bulk fluid-phase endocytosis. (kita2004lossofapm1 pages 8-9, kita2004lossofapm1 pages 4-5, kita2004lossofapm1 pages 2-3) | Direct other AP-1 subunit/whole-complex evidence | Lucifer-yellow uptake showed no detectable general endocytic delay over 30 min in apm1 mutants, whereas secretion and selected-cargo localization were defective. | Moderate for Vas2. Functional assignment follows its verified AP-1 membership, but transport direction and cargo specificity have not been measured directly for Vas2. |
| VPA-sensitive phenotype | vas2/aps1 is directly associated with valproic-acid hypersensitivity and was classified among membrane-trafficking-defective VPA-sensitive mutants. (zhang2013genomewidescreeningfor pages 5-7, zhang2013genomewidescreeningfor pages 1-2) | Direct vas2 evidence | A genome-wide screen tested 3,004 haploid deletion strains at 5 mM VPA for 6 days at 27°C in four repeats; 148 mutants were confirmed VPA-sensitive. Of these, 93 also responded to 30 mM sodium butyrate and 55 were VPA-specific; 17/148 (11.5%) were membrane-trafficking genes. (zhang2013genomewidescreeningfor pages 2-3) | High for phenotype; low-to-moderate for mechanism. The study establishes sensitivity but not a Vas2-specific biochemical VPA target. Sensitivity may arise indirectly from compromised trafficking and cell-wall homeostasis. |
| Syb1 cargo evidence | Loss of the AP-1 μ1 subunit Apm1 prevents normal delivery of the exocytic SNARE Syb1 to polarized secretion sites and causes its accumulation in Golgi/endosomal compartments. (kita2004lossofapm1 pages 8-9, kita2004lossofapm1 pages 1-2) | Direct other AP-1 subunit/whole-complex evidence | Acid-phosphatase reporter secretion was reduced at 27°C and abolished after shift to 36°C or FK506 treatment. (kita2004lossofapm1 pages 4-5) | Moderate as AP-1-pathway evidence; low for direct Vas2 cargo assignment. Syb1 binding to Vas2 was not shown. |
| GPI-anchored cargo evidence | The GPI-anchored proteins Ecm33 and Gaz2 require an intact Apm1-dependent clathrin/post-Golgi pathway for efficient surface delivery; in apm1 deletion cells they accumulate in intracellular Golgi/endosome-like puncta. (jaiseng2012studiesonthe pages 7-8) | Direct other AP-1 subunit/whole-complex evidence | Ecm33 puncta colocalized with FM4-64 and the Golgi/endosome marker Krp1-RFP; Gaz2 likewise shifted from surface/medial localization to intracellular dots. | Moderate for an AP-1-associated route; low for direct Vas2 specificity. The experiments tested apm1, not vas2, and do not establish direct cargo–Vas2 binding. |
| Calcineurin relationship in S. pombe | AP-1-dependent trafficking and calcineurin provide overlapping support for cell integrity and viability: apm1 loss is FK506-sensitive and synthetically lethal with calcineurin deletion. (kita2004lossofapm1 pages 4-5, kita2004lossofapm1 pages 1-2, kita2004lossofapm1 pages 2-3) | Direct other AP-1 subunit/whole-complex evidence | No viable apm1/calcineurin-deletion double mutant was recovered; 1.2 M sorbitol rescued temperature-associated growth/cytokinesis defects but not FK506 sensitivity. (kita2004lossofapm1 pages 11-12) | Moderate for the AP-1 pathway; unproven for Vas2 specifically. No direct vas2–calcineurin genetic or biochemical experiment was retrieved. |
| Recent comparative calcineurin evidence | A January 2024 Candida glabrata study supports a conserved fungal link between AP-1 defects and calcineurin-dependent fitness: aps1Δ, apl2Δ, and arf1Δ mutants were strongly hypersensitive to calcineurin inhibitors. This is comparative evidence, not direct evidence about S. pombe Vas2. (pavesic2024calcineurindependentcontributionsto pages 2-6) | Comparative fungal evidence | 87 FK506-depleted genes were identified; >79% were associated with vesicular trafficking, and 69 were predicted to affect trafficking or ER functions. | Moderate comparative support only. Different organism; relevant calcineurin targets remain unidentified, and results cannot be transferred gene-for-gene without testing. |
| 2023–2024 Vas2-specific literature status | No 2023–2024 mechanistic paper directly characterizing Q9P7N2/SPAP27G11.06c Vas2 was found in the retrieved evidence. The latest directly relevant exact-gene evidence remains the older VPA-genetics literature. | Literature-gap assessment | The recent retrieved AP-1/calcineurin work was in C. glabrata (January 2024), not S. pombe. (pavesic2024calcineurindependentcontributionsto pages 2-6) | Moderate. Absence from the retrieved corpus is not proof that no publication exists; database updates, preprints, or differently indexed studies may have been missed. |
| Homonym warning | Do not conflate Q9P7N2 with Arabidopsis VAS2/GH3.17, an auxin-related enzyme, or with an S. pombe protein called Aps1 reported as a Nudix-type inositol-pyrophosphatase/polyphosphatase. These are distinct proteins despite symbol overlap. (koc2026speciescontextreverses pages 31-32) | Ambiguity control; comparative/off-target literature | No quantitative result from either homonym is applicable to Q9P7N2. | High importance. Use UniProt Q9P7N2, ORF SPAP27G11.06c, organism, and AP-1-small-subunit domains together when selecting literature. |
Table: Evidence-tiered functional annotation of S. pombe Vas2/Q9P7N2, separating direct gene evidence from AP-1 complex inference and comparative fungal findings. The table also flags critical symbol homonyms and current literature gaps.
AP-1 complex sigma subunit Vas2/Aps1 is a conserved, noncatalytic small adaptin predicted to contribute to AP-1 complex assembly and selective cargo sorting in clathrin-associated traffic at Golgi/TGN and endosomal membranes. In S. pombe, Vas2 loss confers valproic-acid sensitivity. AP-1-pathway studies using the μ1 subunit Apm1 support roles in post-Golgi secretion, polarized delivery of Syb1 and GPI-anchored surface proteins, cell-wall integrity, cytokinesis, and vacuole organization, with strong genetic interaction with calcineurin.
The most informative next steps would be endogenous Vas2 fluorescent tagging with quantitative colocalization against TGN and endosome markers; affinity purification or proximity labeling to verify AP-1 partners; side-by-side vas2Δ and other AP-1-subunit mutants; live-cell tracking of Syb1, Ecm33, and Gaz2; rescue with wild-type and domain-mutant Vas2; and genetic/biochemical tests for interaction with calcineurin, Arf/Rab machinery, and clathrin. Direct cargo-binding and structural studies would determine whether Vas2 contributes only to core stability or also participates in sorting-signal recognition.
References
(zhang2013genomewidescreeningfor pages 1-2): Lili Zhang, Ning Ma, Qingbin Liu, and Yan Ma. Genome-wide screening for genes associated with valproic acid sensitivity in fission yeast. PLoS ONE, 8:e68738, Jul 2013. URL: https://doi.org/10.1371/journal.pone.0068738, doi:10.1371/journal.pone.0068738. This article has 26 citations and is from a peer-reviewed journal.
(zhang2013genomewidescreeningfor pages 2-3): Lili Zhang, Ning Ma, Qingbin Liu, and Yan Ma. Genome-wide screening for genes associated with valproic acid sensitivity in fission yeast. PLoS ONE, 8:e68738, Jul 2013. URL: https://doi.org/10.1371/journal.pone.0068738, doi:10.1371/journal.pone.0068738. This article has 26 citations and is from a peer-reviewed journal.
(koc2026speciescontextreverses pages 31-32): Elisa Koc, Lisa Juhran, Visnja Emmerich, Abel Alcázar-Román, Simon M. Bartsch, Adolfo Saiardi, Lasse van Wijlick, Johannes Postma, Thomas Lenz, Dorothea Fiedler, Michael Feldbrügge, Kai Stühler, Ingrid Span, and Ursula Fleig. Species context reverses ppip5k control of fungal morphogenesis and actin organization. bioRxiv, Aug 2026. URL: https://doi.org/10.64898/2026.08.19.745713, doi:10.64898/2026.08.19.745713. This article has 0 citations.
(kita2004lossofapm1 pages 4-5): Ayako Kita, Reiko Sugiura, Hiromi Shoji, Yi He, Lu Deng, Yabin Lu, Susie O. Sio, Kaoru Takegawa, Motoyoshi Sakaue, Hisato Shuntoh, and Takayoshi Kuno. Loss of apm1, the micro1 subunit of the clathrin-associated adaptor-protein-1 complex, causes distinct phenotypes and synthetic lethality with calcineurin deletion in fission yeast. Molecular biology of the cell, 15 6:2920-31, Jun 2004. URL: https://doi.org/10.1091/mbc.e03-09-0659, doi:10.1091/mbc.e03-09-0659. This article has 71 citations and is from a domain leading peer-reviewed journal.
(kita2004lossofapm1 pages 1-2): Ayako Kita, Reiko Sugiura, Hiromi Shoji, Yi He, Lu Deng, Yabin Lu, Susie O. Sio, Kaoru Takegawa, Motoyoshi Sakaue, Hisato Shuntoh, and Takayoshi Kuno. Loss of apm1, the micro1 subunit of the clathrin-associated adaptor-protein-1 complex, causes distinct phenotypes and synthetic lethality with calcineurin deletion in fission yeast. Molecular biology of the cell, 15 6:2920-31, Jun 2004. URL: https://doi.org/10.1091/mbc.e03-09-0659, doi:10.1091/mbc.e03-09-0659. This article has 71 citations and is from a domain leading peer-reviewed journal.
(kita2004lossofapm1 pages 2-3): Ayako Kita, Reiko Sugiura, Hiromi Shoji, Yi He, Lu Deng, Yabin Lu, Susie O. Sio, Kaoru Takegawa, Motoyoshi Sakaue, Hisato Shuntoh, and Takayoshi Kuno. Loss of apm1, the micro1 subunit of the clathrin-associated adaptor-protein-1 complex, causes distinct phenotypes and synthetic lethality with calcineurin deletion in fission yeast. Molecular biology of the cell, 15 6:2920-31, Jun 2004. URL: https://doi.org/10.1091/mbc.e03-09-0659, doi:10.1091/mbc.e03-09-0659. This article has 71 citations and is from a domain leading peer-reviewed journal.
(kita2004lossofapm1 pages 8-9): Ayako Kita, Reiko Sugiura, Hiromi Shoji, Yi He, Lu Deng, Yabin Lu, Susie O. Sio, Kaoru Takegawa, Motoyoshi Sakaue, Hisato Shuntoh, and Takayoshi Kuno. Loss of apm1, the micro1 subunit of the clathrin-associated adaptor-protein-1 complex, causes distinct phenotypes and synthetic lethality with calcineurin deletion in fission yeast. Molecular biology of the cell, 15 6:2920-31, Jun 2004. URL: https://doi.org/10.1091/mbc.e03-09-0659, doi:10.1091/mbc.e03-09-0659. This article has 71 citations and is from a domain leading peer-reviewed journal.
(kita2004lossofapm1 pages 11-12): Ayako Kita, Reiko Sugiura, Hiromi Shoji, Yi He, Lu Deng, Yabin Lu, Susie O. Sio, Kaoru Takegawa, Motoyoshi Sakaue, Hisato Shuntoh, and Takayoshi Kuno. Loss of apm1, the micro1 subunit of the clathrin-associated adaptor-protein-1 complex, causes distinct phenotypes and synthetic lethality with calcineurin deletion in fission yeast. Molecular biology of the cell, 15 6:2920-31, Jun 2004. URL: https://doi.org/10.1091/mbc.e03-09-0659, doi:10.1091/mbc.e03-09-0659. This article has 71 citations and is from a domain leading peer-reviewed journal.
(jaiseng2012studiesonthe pages 7-8): Wurentuya Jaiseng, Yue Fang, Yan Ma, Reiko Sugiura, and Takayoshi Kuno. Studies on the roles of clathrin-mediated membrane trafficking and zinc transporter cis4 in the transport of gpi-anchored proteins in fission yeast. PLoS ONE, 7:e41946, Jul 2012. URL: https://doi.org/10.1371/journal.pone.0041946, doi:10.1371/journal.pone.0041946. This article has 12 citations and is from a peer-reviewed journal.
(zhang2013genomewidescreeningfor pages 5-7): Lili Zhang, Ning Ma, Qingbin Liu, and Yan Ma. Genome-wide screening for genes associated with valproic acid sensitivity in fission yeast. PLoS ONE, 8:e68738, Jul 2013. URL: https://doi.org/10.1371/journal.pone.0068738, doi:10.1371/journal.pone.0068738. This article has 26 citations and is from a peer-reviewed journal.
(pavesic2024calcineurindependentcontributionsto pages 2-6): Matthew W. Pavesic, Andrew N. Gale, Timothy J. Nickels, Abigail A. Harrington, Maya Bussey, and Kyle W. Cunningham. Calcineurin-dependent contributions to fitness in the opportunistic pathogen candida glabrata. Jan 2024. URL: https://doi.org/10.1128/msphere.00554-23, doi:10.1128/msphere.00554-23. This article has 16 citations and is from a peer-reviewed journal.
(pavesic2023regulationofcellular pages 53-62): M Pavesic. Regulation of cellular stresses in yeast cells by calcineurin. Unknown journal, 2023.
(pavesic2023regulationofcellular pages 19-23): M Pavesic. Regulation of cellular stresses in yeast cells by calcineurin. Unknown journal, 2023.