Vacuolar amino acid transporters upregulated by exogenous proline and involved in cellular localization of proline in &lt;i&gt;Saccharomyces cerevisiae&lt;/i&gt;

Nishida, Ikuhisa; Watanabe, Dai; Tsolmonbaatar, Ariunzaya; Kaino, Tomohiro; Ohtsu, Iwao; Takagi, Hiroshi

doi:10.2323/jgam.2016.01.005

Cited by 23 publications

(16 citation statements)

References 38 publications

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“…Based on these results, it was concluded that Fmp12 specifically localizes at the mitochondria. The expression level of Fmp12-yeGFP was not significantly affected by exogenous carbon or nitrogen sources (Figure 1E), although the FMP12 mRNA was previously found to be upregulated by the addition of proline to the medium 10.…”

Section: Resultsmentioning

confidence: 71%

“…Under such a severe nutrient condition, BY4741 wild-type cells in which the auxotrophic mutations were complemented could only slightly grow during 7-day incubation (Figure 1A). Interestingly, among the FMP genes ( FMP12/16/21/27/33/41/45/46/48/52 ) that were upregulated by exogenous proline in our previous study 10, deletion of the FMP12/AIM17 gene was found to markedly enhance the growth on SD-N-C+Pro agar plates (Figure 1A), as well as on SD-C+Pro agar plates, in which proline and ammonium sulfate was added as the sole carbon and nitrogen source, respectively (data not shown). In contrast, overexpression of the FMP12 gene inhibited the growth on SD-N-C+Pro agar plates (Figure 1B).…”

Section: Resultsmentioning

confidence: 71%

“…To find novel regulators of intracellular proline, we previously performed a transcriptomic analysis of the S. cerevisiae put1 mutant in response to exogenous proline 10. As a result, the accumulation of intracellular proline led to downregulation of the proline-synthetic genes and upregulation of the genes that encode the proline-degradative enzymes, the known proline permeases on the plasma membrane, and the Avt proteins associated with bidirectional transport of proline across the vacuolar membrane.…”

Section: Introductionmentioning

confidence: 99%

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Putative mitochondrial α-ketoglutarate-dependent dioxygenase Fmp12 controls utilization of proline as an energy source in Saccharomyces cerevisiae

Nishida¹,

Watanabe²,

Takagi³

2016

Microb Cell

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The amino acid proline functions as a nitrogen source and as a stress protectant in the yeast Saccharomyces cerevisiae. However, utilization of proline as a carbon source in S. cerevisiae cells has not been studied yet. In the process of study on the physiological roles of the found-in-mitochondrial-proteome (FMP) genes in proline metabolism, we found that Δfmp12 cells could grow better than wild-type cells on agar plate medium containing proline as the sole nitrogen and carbon sources. In contrast, overexpression of FMP12 negatively affected cell growth under the same condition. The Fmp12 protein was localized in the mitochondria and was constitutively expressed. Deletion of the genes that encode mitochondrial enzymes, such as proline dehydrogenase (PUT1), Δ1-pyrroline-5-carboxylate dehydrogenase (PUT2), alanine transaminase (ALT1), and α-ketoglutarate dehydrogenase subunit (KGD1), abolished the enhanced cell growth in Δfmp12. These results provided the first evidence that proline can be utilized as a carbon source via the mitochondrial proline metabolic pathway and the subsequent tricarboxylic acid (TCA) cycle in S. cerevisiae. The function of Fmp12, which has a similarity with α-ketoglutarate-dependent dioxygenases of the yeast Candida species and human, might inhibit cell growth by skipping the ATP production step of the TCA cycle.

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Section: Resultsmentioning

confidence: 71%

Section: Resultsmentioning

confidence: 71%

Section: Introductionmentioning

confidence: 99%

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Putative mitochondrial α-ketoglutarate-dependent dioxygenase Fmp12 controls utilization of proline as an energy source in Saccharomyces cerevisiae

Nishida¹,

Watanabe²,

Takagi³

2016

Microb Cell

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“…Avt4 can also export the basic amino acids arginine, lysine, and histidine [193]. Avt3 may additionally export proline, as vacuolar proline levels are higher in avt3Δ cells than wild-type cells [194]. Avt6 exports glutamate and aspartate from vacuoles [191], whereas recent work has demonstrated that Avt7 may be involved in efflux of glutamine and proline [195].…”

Section: Efflux Of Amino Acidsmentioning

confidence: 99%

Vacuolar hydrolysis and efflux: current knowledge and unanswered questions

Parzych

Klionsky

2018

Autophagy

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Hydrolysis within the vacuole in yeast and the lysosome in mammals is required for the degradation and recycling of a multitude of substrates, many of which are delivered to the vacuole/lysosome by autophagy. In humans, defects in lysosomal hydrolysis and efflux can have devastating consequences, and contribute to a class of diseases referred to as lysosomal storage disorders. Despite the importance of these processes, many of the proteins and regulatory mechanisms involved in hydrolysis and efflux are poorly understood. In this review, we describe our current knowledge of the vacuolar/lysosomal degradation and efflux of a vast array of substrates, focusing primarily on what is known in the yeast Saccharomyces cerevisiae. We also highlight many unanswered questions, the answers to which may lead to new advances in the treatment of lysosomal storage disorders.

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“…It is thought that the putative vacuolar permease Atg22 is the protein that may be responsible for this transport. This protein may cooperate with two other vacuolar permeases Avt3 and Avt4 [123][124][125], which mediate the transport of leucine and other amino acids from the vacuole to the cytoplasm [123][124][125][126]. Nevertheless, the involvement of Avt3 and Avt4 in the transport of amino acids derived from the degradation of the autophagic body during autophagy in yeast is still hypothetical (Figure 2, Table 3) [123][124][125].…”

Section: Degradation Of the Autophagic Body And Metabolite Efflux Fromentioning

confidence: 99%

Completing Autophagy: Formation and Degradation of the Autophagic Body and Metabolite Salvage in Plants

Stefaniak

Wojtyla

Pietrowska‐Borek

et al. 2020

IJMS

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Autophagy is an evolutionarily conserved process that occurs in yeast, plants, and animals. Despite many years of research, some aspects of autophagy are still not fully explained. This mostly concerns the final stages of autophagy, which have not received as much interest from the scientific community as the initial stages of this process. The final stages of autophagy that we take into consideration in this review include the formation and degradation of the autophagic bodies as well as the efflux of metabolites from the vacuole to the cytoplasm. The autophagic bodies are formed through the fusion of an autophagosome and vacuole during macroautophagy and by vacuolar membrane invagination or protrusion during microautophagy. Then they are rapidly degraded by vacuolar lytic enzymes, and products of the degradation are reused. In this paper, we summarize the available information on the trafficking of the autophagosome towards the vacuole, the fusion of the autophagosome with the vacuole, the formation and decomposition of autophagic bodies inside the vacuole, and the efflux of metabolites to the cytoplasm. Special attention is given to the formation and degradation of autophagic bodies and metabolite salvage in plant cells.

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Vacuolar amino acid transporters upregulated by exogenous proline and involved in cellular localization of proline in <i>Saccharomyces cerevisiae</i>

Cited by 23 publications

References 38 publications

Putative mitochondrial α-ketoglutarate-dependent dioxygenase Fmp12 controls utilization of proline as an energy source in Saccharomyces cerevisiae

Putative mitochondrial α-ketoglutarate-dependent dioxygenase Fmp12 controls utilization of proline as an energy source in Saccharomyces cerevisiae

Vacuolar hydrolysis and efflux: current knowledge and unanswered questions

Completing Autophagy: Formation and Degradation of the Autophagic Body and Metabolite Salvage in Plants

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