What is the clinical evidence from this study?

Study design: Other. Population: Potassium homeostasis. Intervention: Phosphorylation of S44 in ROMK1. Primary outcome: Channel expression and cell surface delivery.

What question did this study set out to answer?

To elucidate the mechanism by which phosphorylation of the amino-terminal serine 44 regulates the cell surface expression and endoplasmic reticulum trafficking of the ROMK1 potassium channel.

June 29, 2005Proceedings of the National Academy of Sciences

Phosphorylation-regulated endoplasmic reticulum retention signal in the renal outer-medullary K + channel (ROMK)

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Key result

Phosphorylation of S44 in the NH2 terminus of ROMK1 increases cell surface delivery by suppressing a COOH-terminal endoplasmic reticulum retention signal.

Population

Preclinical model investigating the renal outer-medullary K+ channel (ROMK; Kir1.1)

Design

Preclinical

Authors

AOAnthony O’ConnellSugar Research Australia (Australia)QLQiang LengCapital Medical University KDKe DongYale University

Discussion

Member takes

Implication

No immediate clinical implications for potassium disorders; leaves open in vivo relevance of S44 phosphorylation for ROMK trafficking.

Key Points

To elucidate the mechanism by which phosphorylation of the amino-terminal serine 44 regulates the cell surface expression and endoplasmic reticulum trafficking of the ROMK1 potassium channel.
Evaluated the effect of serine 44 (S44) phosphorylation by PKA and SGK1 on ROMK1 trafficking from the endoplasmic reticulum to the cell surface.
Analyzed structural models based on inward rectifier potassium channel x-ray crystallography to assess interactions between the amino and carboxyl termini.
Phosphorylation of S44 in the amino terminus suppressed a carboxyl-terminal endoplasmic reticulum (ER) retention signal, thereby promoting channel delivery to the plasma membrane.
Identified inter-subunit interactions between the amino terminus and adjacent distal carboxyl terminus, suggesting phosphorylation acts as a folding checkpoint essential for proper channel gating.

Structured PICO

Population

Preclinical model investigating the renal outer-medullary K+ channel (ROMK; Kir1.1)

Intervention

Phosphorylation of S44 in the NH2 terminus of ROMK1 by PKA and serum- and glucocorticoid-inducible kinase-1

Outcome

Cell surface delivery and expression of functional ROMK channels

NH2-terminal phosphorylation modifies a COOH-terminal ER retention signal in ROMK1, serving as a checkpoint for proper subunit folding and rapid delivery to the plasma membrane.

Cite This Study

O’Connell et al. (2005) studied Potassium homeostasis. Phosphorylation of S44 in ROMK1 was evaluated on Channel expression and cell surface delivery. Phosphorylation of S44 in the NH2 terminus of ROMK1 increases cell surface delivery by suppressing a COOH-terminal endoplasmic reticulum retention signal.

synapsesocial.com/papers/6a08d68b720b08f65a5b6cc9 https://doi.org/10.1073/pnas.0504332102

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June 29, 2005Proceedings of the National Academy of Sciences

Phosphorylation-regulated endoplasmic reticulum retention signal in the renal outer-medullary K + channel (ROMK)

View Full Paper

Ask AI

Bookmark

Key result

Phosphorylation of S44 in the NH2 terminus of ROMK1 increases cell surface delivery by suppressing a COOH-terminal endoplasmic reticulum retention signal.

Population

Preclinical model investigating the renal outer-medullary K+ channel (ROMK; Kir1.1)

Design

Preclinical

Authors

AOAnthony O’ConnellSugar Research Australia (Australia)QLQiang LengCapital Medical University KDKe DongYale University

Discussion

Member takes

Implication

No immediate clinical implications for potassium disorders; leaves open in vivo relevance of S44 phosphorylation for ROMK trafficking.

Key Points

To elucidate the mechanism by which phosphorylation of the amino-terminal serine 44 regulates the cell surface expression and endoplasmic reticulum trafficking of the ROMK1 potassium channel.
Evaluated the effect of serine 44 (S44) phosphorylation by PKA and SGK1 on ROMK1 trafficking from the endoplasmic reticulum to the cell surface.
Analyzed structural models based on inward rectifier potassium channel x-ray crystallography to assess interactions between the amino and carboxyl termini.
Phosphorylation of S44 in the amino terminus suppressed a carboxyl-terminal endoplasmic reticulum (ER) retention signal, thereby promoting channel delivery to the plasma membrane.
Identified inter-subunit interactions between the amino terminus and adjacent distal carboxyl terminus, suggesting phosphorylation acts as a folding checkpoint essential for proper channel gating.

Structured PICO

Population

Preclinical model investigating the renal outer-medullary K+ channel (ROMK; Kir1.1)

Intervention

Phosphorylation of S44 in the NH2 terminus of ROMK1 by PKA and serum- and glucocorticoid-inducible kinase-1

Outcome

Cell surface delivery and expression of functional ROMK channels

NH2-terminal phosphorylation modifies a COOH-terminal ER retention signal in ROMK1, serving as a checkpoint for proper subunit folding and rapid delivery to the plasma membrane.

Cite This Study

synapsesocial.com/papers/6a08d68b720b08f65a5b6cc9 https://doi.org/10.1073/pnas.0504332102

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

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