THE EFFECT OF PHOSPHORYLATION AND DEPHOSPHORYLATION OF THE SERINE RESIDUE (S362) ON ROMK2 (KIR1.1B) ENDOCYTOSIS

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HAJI HASHEMI S.

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Journal: Journal of Arak University Medical Sciences Year:2009 | Volume:12 | Issue:1 (46) Page(s): 19-28

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Title

THE EFFECT OF PHOSPHORYLATION AND DEPHOSPHORYLATION OF THE SERINE RESIDUE (S362) ON ROMK2 (KIR1.1B) ENDOCYTOSIS

Author(s)

HAJI HASHEMI S. | Issue Writer Certificate

Keywords

POTASSIUM CHANNELQ3

ROMK2Q3

S362A MUTANTQ3

S362D MUTANTQ3

BFAQ3

PDZ DOMAINQ3

PHOSPHORYLATIONQ3

Abstract

Background: In this study, the effects of S362A and S362D mutations on the membrane turnover and the stability of ROMK2 channel when expressing in Xenopus laevis oocytes were examined.Methods and Materials:In this experimental study, oocytes were isolated by standard protocols using collagens (Type 1A). Mutations of the cytoplasmic termini of ROMK2 were constructed using the quick-change approach for site-directed mutagenesis. Xenopus oocytes were injected with cRNA encoding ROMK2 or S362A or S362D MUTANT three days prior to treatment with BFA solution (time 0). Brefeldin A (BFA) was added to the OR3 medium (+BFA) at concentrations of 25mM (inhibit insertion of new proteins into the cell membrane) or ethanol as BFA vehicle (-BFA). Two-electrode voltage clamp (TEVC) was used to measure oocyte ROMK-dependent currents and membrane potential.Results: In oocytes was expressing ROMK2 and/or the S362A MUTANT, there was significant reduce in current and membrane voltage of K. The fractional currents for ROMK2 and S362D MUTANT demonstrated a slight difference 48h following treatment of oocytes with BFA, 0.16±0.05 (n=18) and 0.11±0.05 (n=18) respectively. This was; however, significantly different from the fractional current of S362A MUTANT which stood at 0.96±0.05 (n=24).Conclusion: Mutant Serine residue S362A which causes PHOSPHORYLATION in endocytosis and helps determine the number of ROMK2, plays an important part in PDZ DOMAIN.

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APA: Copy

HAJI HASHEMI, S.. (2009). THE EFFECT OF PHOSPHORYLATION AND DEPHOSPHORYLATION OF THE SERINE RESIDUE (S362) ON ROMK2 (K_IR1.1B) ENDOCYTOSIS. ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ), 12(1 (46)), 19-28. SID. https://sid.ir/paper/69040/en

Vancouver: Copy

HAJI HASHEMI S.. THE EFFECT OF PHOSPHORYLATION AND DEPHOSPHORYLATION OF THE SERINE RESIDUE (S362) ON ROMK2 (K_IR1.1B) ENDOCYTOSIS. ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ)[Internet]. 2009;12(1 (46)):19-28. Available from: https://sid.ir/paper/69040/en

IEEE: Copy

S. HAJI HASHEMI, “THE EFFECT OF PHOSPHORYLATION AND DEPHOSPHORYLATION OF THE SERINE RESIDUE (S362) ON ROMK2 (K_IR1.1B) ENDOCYTOSIS,” ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ), vol. 12, no. 1 (46), pp. 19–28, 2009, [Online]. Available: https://sid.ir/paper/69040/en

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