Interaction of the Brain-Selective Sulfotransferase SULT4A1 with Other Cytosolic Sulfotransferases: Effects on Protein Expression and Function

Idris, Misgana; Mitchell, Deanne J.; Gordon, Richard D.; Sidharthan, Neelima P.; Butcher, Neville J.; Minchin, Rodney F.

doi:10.1124/dmd.119.089714

Cited by 10 publications

(16 citation statements)

References 44 publications

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“…44,45,47 Interestingly, DCNP is known to lower PAPS levels 54 and inhibit the SULT1A1 isoform, but not the SULT1A3 isoform, 15,49,55 which is also expressed in SK-N-MC cells. 12,52,53 As such, this provides strong evidence that STS-3 is a reporter of SULT1A1 activity in this cell line. Indeed, the fluorescence imaging also highlights how the reported activity can vary from cell-to-cell.…”

Section: Main Textsupporting

confidence: 54%

“…To validate STS-3, we selected the human SK-N-MC neuroepithelial cancer cell line, which has been previously reported to express SULT1A1. 52,53 First, SK-N-MC cells were treated with either a DMSO vehicle control or 10 μM of STS-3 for 4 h at 37 °C in serum free media, followed by lysis and analysis with fluorescence-based high-performance liquid chromatography (HPLC).…”

Section: Main Textmentioning

confidence: 99%

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An Activity-Based Fluorescent Sensor for the Detection of the Phenol Sulfotransferase SULT1A1 in Living Cells

Baglia

Mills

Mitra

et al. 2020

Preprint

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<p>The biological activation and incorporation of inorganic sulfate proceeds via a process known as sulfurylation. Transfer of a sulfuryl moiety from the activated sulfate donor, 3’-phosphoadenosine-5’-phosphosulfate (PAPS), to hydroxy-containing substrates by human phenol sulfotransferases (SULT1 family) alters substrate solubility and charge to affect the metabolism of endogenous metabolites, xenobiotics, and drugs. Current methods to monitor SULT1 activity in living cells primarily rely on radiolabeling and/or cell extractions, but these methods do not provide a direct readout of enzyme activity with a dynamic, temporally resolved spatial map in live, intact cells. To fill this gap, here, we present the development, computational modeling, <i>in vitro</i> enzymology, and biological application of Sulfotransferase Sensor-3, STS-3, an activity-based fluorescent sensor for SULT1A1, the most widely expressed and promiscuous SULT1 isoform. </p>

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Section: Main Textsupporting

confidence: 54%

Section: Main Textmentioning

confidence: 99%

An Activity-Based Fluorescent Sensor for the Detection of the Phenol Sulfotransferase SULT1A1 in Living Cells

Baglia

Mills

Mitra

et al. 2020

Preprint

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show abstract

“…46,47,49 Interestingly, DCNP is known to lower PAPS levels 56 and inhibit the SULT1A1 isoform, but not the SULT1A3 isoform, 15,51,57 which is also expressed in SK-N-MC cells. 12,54,55 As such, this provides strong evidence that STS-3 is a reporter of SULT1A1 activity in this cell line. Indeed, the fluorescence imaging also highlights how the reported activity can vary from cell-to-cell.…”

supporting

confidence: 54%

“…To validate STS-3, we selected the human SK-N-MC neuroepithelial cancer cell line, which has been previously reported to express SULT1A1. 54,55 First, SK-N-MC cells were treated with either a DMSO vehicle control or 10 mM of STS-3 for 4 h at 37 1C in serum-free media, followed by lysis and analysis with fluorescence-based high-performance liquid chromatography (HPLC) (Fig. 4 and Fig.…”

mentioning

confidence: 99%

An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells

et al. 2021

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“…Heterodimers could provide a mechanism by which substrates of one SULT could affect sulfation of another. Also, SULT4A1 alone has been hypothesized to play important roles in neuronal development, by heterodimerizing with and regulating the activity of other SULTs (Idris et al, 2020).…”

Section: Substrate Specificity Of Sultsmentioning

confidence: 99%

From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function

Pedersen

et al. 2022

Drug Metab Dispos

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Sulfotransferases are ubiquitous enzymes that transfer a sulfo group (SO 3 ) from the universal cofactor donor PAPS to a broad range of acceptor substrates. In humans, the cytosolic sulfotransferases (SULTs) are involved in the sulfation of endogenous compounds such as steroids, neurotransmitters, hormones and bile acids as well as xenobiotics including drugs, toxins and environmental chemicals. The Golgi associated membrane-bound sulfotransferases are involved in post-translational modification of macromolecules from glycosaminoglycans to proteins. The sulfation of small molecules can have profound biological effects on the functionality of the acceptor, including activation, deactivation or enhanced metabolism and elimination. Sulfation of macromolecules has been shown to regulate a number of physiological and pathophysiological pathways by enhancing binding affinity to regulatory proteins or binding partners. Over the last 25 years, crystal structures of these enzymes have provided a wealth of information on the mechanisms of this process and the specificity of these enzymes. This review will focus on the general commonalities of the sulfotransferases, from enzyme structure to catalytic mechanism as well as providing examples into how structural information is being utilized to either design drugs that inhibit sulfotransferases or to modify the enzymes to improve drug synthesis.

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Interaction of the Brain-Selective Sulfotransferase SULT4A1 with Other Cytosolic Sulfotransferases: Effects on Protein Expression and Function

Abstract: Interaction of the brain-selective sulfotransferase SULT4A1 with other cytosolic sulfotransferases: effects on protein expression and function.

Cited by 10 publications

References 44 publications

An Activity-Based Fluorescent Sensor for the Detection of the Phenol Sulfotransferase SULT1A1 in Living Cells

An Activity-Based Fluorescent Sensor for the Detection of the Phenol Sulfotransferase SULT1A1 in Living Cells

An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells

From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function

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