2018
DOI: 10.1105/tpc.18.00512
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PAPST2 Plays Critical Roles in Removing the Stress Signaling Molecule 3′-Phosphoadenosine 5′-Phosphate from the Cytosol and Its Subsequent Degradation in Plastids and Mitochondria

Abstract: The compartmentalization of PAPS (the sulfate donor 39-phosphoadenosine 59-phosphosulfate) synthesis (mainly in plastids), PAPS consumption (in the cytosol), and PAP (the stress signaling molecule 39-phosphoadenosine 59-phosphate) degradation (in plastids and mitochondria) requires organellar transport systems for both PAPS and PAP. The plastidial transporter PAPST1 (PAPS TRANSPORTER1) delivers newly synthesized PAPS from the stroma to the cytosol. We investigated the activity of PAPST2, the closest homolog of… Show more

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Cited by 23 publications
(30 citation statements)
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“…Yet, inferring in vivo function from in vitro data on transport specificity data is known to be problematic and has prevented capture of the biological importance of transport of other substrates. For example, PAPST1 and PAPST2, which are 78% identical in amino acid sequence, both transport 3′-phosphoadenosine 5′-phosphate (PAP) and 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in liposomes with only slight differences in their efficiency in driving ATP exchange (63). However, their true in vivo function was revealed only after additional genetic, biochemical and metabolomic approaches were employed: PAPST1 being responsible for the majority of PAPS/PAP transport to regulate glucosinolate biosynthesis in plastids, while PAPST2 fulfils a stress signalling role through PAP/AT(D)P exchange in chloroplasts and mitochondria (63, 64).…”
Section: Discussionmentioning
confidence: 99%
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“…Yet, inferring in vivo function from in vitro data on transport specificity data is known to be problematic and has prevented capture of the biological importance of transport of other substrates. For example, PAPST1 and PAPST2, which are 78% identical in amino acid sequence, both transport 3′-phosphoadenosine 5′-phosphate (PAP) and 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in liposomes with only slight differences in their efficiency in driving ATP exchange (63). However, their true in vivo function was revealed only after additional genetic, biochemical and metabolomic approaches were employed: PAPST1 being responsible for the majority of PAPS/PAP transport to regulate glucosinolate biosynthesis in plastids, while PAPST2 fulfils a stress signalling role through PAP/AT(D)P exchange in chloroplasts and mitochondria (63, 64).…”
Section: Discussionmentioning
confidence: 99%
“…For example, PAPST1 and PAPST2, which are 78% identical in amino acid sequence, both transport 3′-phosphoadenosine 5′-phosphate (PAP) and 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in liposomes with only slight differences in their efficiency in driving ATP exchange (63). However, their true in vivo function was revealed only after additional genetic, biochemical and metabolomic approaches were employed: PAPST1 being responsible for the majority of PAPS/PAP transport to regulate glucosinolate biosynthesis in plastids, while PAPST2 fulfils a stress signalling role through PAP/AT(D)P exchange in chloroplasts and mitochondria (63, 64). In a similar way, while liposomes showed the ability of DIC2 to transport a variety of dicarboxylates and even citrate, albeit poorly (24), they could not accurately predict apparent specificity or directionality of transport in intact mitochondria (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…Localization links AtPAPST2 to SAL1, which is also present in plastids and mitochondria. Thus, it seems that AtPAPST1 has a major role in exporting PAPS from chloroplast to cytosol for sulfation reactions and AtPAPST2 in importing PAP into the organelles for degradation by SAL1 (157). It also seems that the two transporters, AtPAPST1 and AtPAPST2, are not sufficient to explain all phenotypes connected to movement of PAPS and PAP between cytosol and the organelles, particularly the accumulation of glucosinolates and their desulfo-precursors.…”
Section: Jbc Reviews: Green and Red Sulfation Pathwaysmentioning
confidence: 98%
“…The loss-of-function mutant papst1 accumulates desulfo-glucosinolate precursors and shows decreased glucosinolate levels similar to but to a lower extent than apk1 apk2, suggesting the existence of a second plastidic PAPS transporter. Indeed, AtPAPST2 was recently identified in Arabidopsis as a transporter located dually in membranes of chloroplasts and mitochondria (157). The AtPAPST2 gene is not co-expressed with glucosinolate genes, and its loss had only a minor effect on glucosinolate accumulation (157).…”
Section: Jbc Reviews: Green and Red Sulfation Pathwaysmentioning
confidence: 99%
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