Literature DB >> 16731837

Kir6.2 mutations associated with neonatal diabetes reduce expression of ATP-sensitive K+ channels: implications in disease mechanism and sulfonylurea therapy.

Chia-Wei Lin1, Yu-Wen Lin, Fei-Fei Yan, Jillene Casey, Malini Kochhar, Emily B Pratt, Show-Ling Shyng.   

Abstract

Heterozygous missense mutations in the pore-forming subunit Kir6.2 of ATP-sensitive K(+) channels (K(ATP) channels) have recently been shown to cause permanent neonatal diabetes mellitus (PNDM). Functional studies demonstrated that PNDM mutations reduce K(ATP) channel sensitivity to ATP inhibition, resulting in gain of channel function. However, the impact of these mutations on channel expression has not been examined. Here, we show that PNDM mutations, including Q52R, V59G, V59M, R201C, R201H, and I296L, not only reduce channel ATP sensitivity but also impair channel expression at the cell surface to varying degrees. By tagging the PNDM Kir6.2 mutant V59G or R201H with an additional mutation, N160D, that confers voltage-dependent polyamine block of K(ATP) channels, we demonstrate that in simulated heterozygous state, all surface channels are either wild-type or heteromeric channels containing both wild-type and mutant Kir6.2 subunits. Comparison of the various PNDM mutations in their effects on channel nucleotide sensitivity and expression, as well as disease phenotype, suggests that both channel-gating defect and expression level may play a role in determining disease severity. Interestingly, sulfonylureas significantly increase surface expression of certain PNDM mutants, suggesting that the efficacy of sulfonylurea therapy may be compromised by the effect of these drugs on channel expression.

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Year:  2006        PMID: 16731837     DOI: 10.2337/db05-1571

Source DB:  PubMed          Journal:  Diabetes        ISSN: 0012-1797            Impact factor:   9.461


  23 in total

1.  Differential roles for SUR subunits in KATP channel membrane targeting and regulation.

Authors:  Thomas J Hund; Peter J Mohler
Journal:  Am J Physiol Heart Circ Physiol       Date:  2010-11-05       Impact factor: 4.733

2.  Structurally distinct ligands rescue biogenesis defects of the KATP channel complex via a converging mechanism.

Authors:  Prasanna K Devaraneni; Gregory M Martin; Erik M Olson; Qing Zhou; Show-Ling Shyng
Journal:  J Biol Chem       Date:  2015-01-30       Impact factor: 5.157

3.  Neonatal diabetes caused by mutations in sulfonylurea receptor 1: interplay between expression and Mg-nucleotide gating defects of ATP-sensitive potassium channels.

Authors:  Qing Zhou; Intza Garin; Luis Castaño; Jesús Argente; Ma Teresa Muñoz-Calvo; Guiomar Perez de Nanclares; Show-Ling Shyng
Journal:  J Clin Endocrinol Metab       Date:  2010-09-01       Impact factor: 5.958

4.  A role of the sulfonylurea receptor 1 in endocytic trafficking of ATP-sensitive potassium channels.

Authors:  Cathrin E Bruederle; Joel Gay; Show-Ling Shyng
Journal:  Traffic       Date:  2011-07-03       Impact factor: 6.215

5.  Congenital hyperinsulinism associated ABCC8 mutations that cause defective trafficking of ATP-sensitive K+ channels: identification and rescue.

Authors:  Fei-Fei Yan; Yu-Wen Lin; Courtney MacMullen; Arupa Ganguly; Charles A Stanley; Show-Ling Shyng
Journal:  Diabetes       Date:  2007-06-15       Impact factor: 9.461

6.  Ankyrin regulates KATP channel membrane trafficking and gating in excitable cells.

Authors:  Crystal F Kline; Thomas J Hund; Peter J Mohler
Journal:  Channels (Austin)       Date:  2010-01-16       Impact factor: 2.581

7.  Role of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complex.

Authors:  Fei-Fei Yan; Emily B Pratt; Pei-Chun Chen; Fang Wang; William R Skach; Larry L David; Show-Ling Shyng
Journal:  Mol Biol Cell       Date:  2010-04-28       Impact factor: 4.138

8.  Analysis of two KCNJ11 neonatal diabetes mutations, V59G and V59A, and the analogous KCNJ8 I60G substitution: differences between the channel subtypes formed with SUR1.

Authors:  Marcus Winkler; Rebekka Lutz; Ulrich Russ; Ulrich Quast; Joseph Bryan
Journal:  J Biol Chem       Date:  2009-01-12       Impact factor: 5.157

9.  Leptin regulates KATP channel trafficking in pancreatic β-cells by a signaling mechanism involving AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA).

Authors:  Pei-Chun Chen; Yelena N Kryukova; Show-Ling Shyng
Journal:  J Biol Chem       Date:  2013-10-07       Impact factor: 5.157

Review 10.  Neonatal diabetes mellitus.

Authors:  Lydia Aguilar-Bryan; Joseph Bryan
Journal:  Endocr Rev       Date:  2008-04-24       Impact factor: 19.871

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