Molecular Dissection of the Butyrate Action Revealed the Involvement of Mitogen-Activated Protein Kinase in Cystic Fibrosis Transmembrane Conductance Regulator Biogenesis

Sugita, Makoto; Kongo, Hiroyasu; Shiba, Yoshiki

doi:10.1124/mol.104.001008

Cited by 10 publications

(5 citation statements)

References 45 publications

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“…The current study demonstrates that inhibition of ERK1/2 and JNK MAPK did not affect the amount of apical membrane ⌬F508-CFTR protein in two 4-PBA-treated ⌬F508-CFTR lung cells. Our data are in good agreement with a report showing that the activation of ERK1/2 in Cos7 cells augmented the biogenesis and trafficking of wild-type-CFTR, but not ⌬F508-CFTR protein (Sugita et al, 2004). Reports have identified more than 100 CFTR-interacting proteins required for folding and function of CFTR and considered CFTR as a molecule involved in signal transduction through specific interactions between its intracytoplasmic domain and various proteins such as calnexin, EBP50, and NHERF2 (Wang et al, 2006).…”

Section: Discussionsupporting

confidence: 82%

Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH₂-Terminal Kinase Signaling

Roque¹,

Boncoeur²,

Saint‐Criq³

et al. 2008

J Pharmacol Exp Ther

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Section: Discussionsupporting

confidence: 82%

Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH₂-Terminal Kinase Signaling

Roque¹,

Boncoeur²,

Saint‐Criq³

et al. 2008

J Pharmacol Exp Ther

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“…These data provide evidence that the ERK1/2 pathway could participate in CFTR activation. A relationship between ERK1/2/MAPKK activation and butyrate-induced expression of CFTR was previously demonstrated by Sugita et al (38). According to their results, the integrity of the R domain of CFTR could be important in this regulation, involving active ERK1/2/MAPK in the biogenesis of the protein.…”

Section: Discussionmentioning

confidence: 61%

CFTR mediates apoptotic volume decrease and cell death by controlling glutathione efflux and ROS production in cultured mice proximal tubules

L’Hoste

Chargui

Belfodil

et al. 2010

American Journal of Physiology-Renal Physiology

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We have previously shown that despite the presence of mRNA encoding CFTR, renal proximal cells do not exhibit cAMP-sensitive Cl(-) conductance (Rubera I, Tauc M, Bidet M, Poujeol C, Cuiller B, Watrin A, Touret N, Poujeol P. Am J Physiol Renal Physiol 275: F651-F663, 1998). Nevertheless, in these cells, CFTR plays a crucial role in the control of the volume-sensitive outwardly rectifying (VSOR) activated Cl(-) currents during hypotonic shock. The aim of this study was to determine the role of CFTR in the regulation of apoptosis volume decrease (AVD) and the apoptosis phenomenon. For this purpose, renal cells were immortalized from primary cultures of proximal convoluted tubules from cftr(+/+) and cftr(-/-) mice. Apoptosis was induced by staurosporine (STS; 1 microM). Cell volume, Cl(-) conductance, caspase-3 activity, intracellular level of reactive oxygen species (ROS), and glutathione content (GSH/GSSG) were monitored during AVD. In cftr(+/+) cells, AVD and caspase-3 activation were strongly impaired by conventional Cl(-) channel blockers and by a specific CFTR inhibitor (CFTR(inh)-172; 5 microM). STS induced activation of CFTR conductance within 15 min, which was progressively replaced by VSOR Cl(-) currents after 60 min of exposure. In parallel, STS induced an increase in ROS content in the time course of VSOR Cl(-) current activation. This increase was impaired by CFTR(inh)-172 and was not observed in cftr(-/-) cells. Furthermore, the intracellular GSH/GSSG content decreased during STS exposure in cftr(+/+) cells only. In conclusion, CFTR could play a key role in the cascade of events leading to apoptosis. This role probably involves control of the intracellular ROS balance by some CFTR-dependent modulation of GSH concentration.

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“…Sodium Butyrate (NaBu) has been shown to rescue unfolded membrane‐spanning proteins from ER retention and premature degradation, and to restore trafficking and wild‐type function. Unfolding can be caused by disease‐associated mutations (Sugita et al, ; Danilov et al, ). In our experiments, cells cultured with NaBu exhibited increased amounts of TMEM16E‐GFP and TMEM16E gdd ‐GFP (Fig.…”

Section: Resultsmentioning

confidence: 99%

TMEM16E (GDD1) Exhibits Protein Instability and Distinct Characteristics in Chloride Channel/Pore Forming Ability

Tran

Tobiume

Hirono

et al. 2013

Journal Cellular Physiology

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TMEM16E/GDD1 has been shown to be responsible for the bone-related late-onset disease gnathodiaphyseal dysplasia (GDD), with the dominant allele (TMEM16E(gdd) ) encoding a missense mutation at Cys356. Additionally, several recessive loss-of-function alleles of TMEM16E also cause late-onset limb girdle muscular dystrophy. In this study, we found that TMEM16E was rapidly degraded via the proteasome pathway, which was rescued by inhibition of the PI3K pathway and by the chemical chaperone, sodium butyrate. Moreover, TMEM16E(gdd) exhibited lower stability than TMEM16E, but showed similar propensity to be rescued. TMEM16E did not exhibit cell surface calcium-dependent chloride channel (CaCC) activity, which was originally identified in TMEM16A and TMEM16B, due to their intracellular vesicle distribution. A putative pore-forming domain of TMEM16E, which shared 39.8% similarity in 98 amino acids with TMEM16A, disrupted CaCC activity of TMEM16A via domain swapping. However, the Thr611Cys mutation in the swapped domain, which mimicked conserved cysteine residues between TMEM16A and TMEM16B, reconstituted CaCC activity. In addition, the GDD-causing cysteine mutation made in TMEM16A drastically altered CaCC activity. Based on these findings, TMEM16E possesses distinct function other than CaCC and another protein-stabilizing machinery toward the TMEM16E and TMEM16E(gdd) proteins should be considered for the on-set regulation of their phenotypes in tissues.

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Molecular Dissection of the Butyrate Action Revealed the Involvement of Mitogen-Activated Protein Kinase in Cystic Fibrosis Transmembrane Conductance Regulator Biogenesis

Cited by 10 publications

References 45 publications

Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH₂-Terminal Kinase Signaling

Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH₂-Terminal Kinase Signaling

CFTR mediates apoptotic volume decrease and cell death by controlling glutathione efflux and ROS production in cultured mice proximal tubules

TMEM16E (GDD1) Exhibits Protein Instability and Distinct Characteristics in Chloride Channel/Pore Forming Ability

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Molecular Dissection of the Butyrate Action Revealed the Involvement of Mitogen-Activated Protein Kinase in Cystic Fibrosis Transmembrane Conductance Regulator Biogenesis

Cited by 10 publications

References 45 publications

Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH2-Terminal Kinase Signaling

Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH2-Terminal Kinase Signaling

CFTR mediates apoptotic volume decrease and cell death by controlling glutathione efflux and ROS production in cultured mice proximal tubules

TMEM16E (GDD1) Exhibits Protein Instability and Distinct Characteristics in Chloride Channel/Pore Forming Ability

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Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH₂-Terminal Kinase Signaling

Proinflammatory Effect of Sodium 4-Phenylbutyrate in ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator Lung Epithelial Cells: Involvement of Extracellular Signal-Regulated Protein Kinase 1/2 and c-Jun-NH₂-Terminal Kinase Signaling