ArticleThe Journal of biological chemistry2010
Diverse pathways for maturation of the Na,K-ATPase β1 and β2 subunits in the endoplasmic reticulum of Madin-Darby canine kidney cells.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Na,K-ATPase Expression Can Be Limited Post-Transcriptionally: A Test of the Role of the Beta Subunit, and a Review of Evidence.International journal of molecular sciences · 2024Review
- Identified and potential internalization signals involved in trafficking and regulation of NaMolecular and cellular biochemistry · 2024Review
- Maturation of the Na,K-ATPase in the Endoplasmic Reticulum in Health and Disease.The Journal of membrane biology · 2021Article
- Molecular mechanisms of Na,K-ATPase dysregulation driving alveolar epithelial barrier failure in severe COVID-19.American journal of physiology. Lung cellular and molecular physiology · 2021Article
- Article
- Hypercapnia Impairs Na,K-ATPase Function by Inducing Endoplasmic Reticulum Retention of the β-Subunit of the Enzyme in Alveolar Epithelial Cells.International journal of molecular sciences · 2020Article
- In systemic lupus erythematosus anti-dsDNA antibodies can promote thrombosis through direct platelet activation.Journal of autoimmunity · 2020Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- A CASPR1-ATP1B3 protein interaction modulates plasma membrane localization of NaThe Journal of biological chemistry · 2019Article
- Article
- Age-related changes in Na, K-ATPase expression, subunit isoform selection and assembly in the stria vascularis lateral wall of mouse cochlea.Hearing research · 2018Article
- Noradrenergic β-Adrenoceptor-Mediated Intracellular Molecular Mechanism of Na-K ATPase Subunit Expression in C6 Cells.Cellular and molecular neurobiology · 2018Article
- Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart: DISTINCT FUNCTIONAL PROPERTIES AND ISOFORM-SELECTIVE INHIBITORS.The Journal of biological chemistry · 2016Article
- Septin oligomerization regulates persistent expression of ErbB2/HER2 in gastric cancer cells.The Biochemical journal · 2016Article
- Septin dynamics are essential for exocytosis.The Journal of biological chemistry · 2015Article
- Subunit isoform selectivity in assembly of Na,K-ATPase α-β heterodimers.The Journal of biological chemistry · 2012Article
- Functional regulation of sugar assimilation by N-glycan-specific interaction of pancreatic α-amylase with glycoproteins of duodenal brush border membrane.The Journal of biological chemistry · 2012Article
- Epithelial junctions depend on intercellular trans-interactions between the Na,K-ATPase β₁ subunits.The Journal of biological chemistry · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Proper folding of the Na,K-ATPase β subunits followed by assembly with the α subunits is necessary for their export from the endoplasmic reticulum (ER). Here we examine roles of the ER lectin chaperone, calnexin, and non-lectin chaperone, BiP, in folding and quality control of the β(1) and β(2) subunits in Madin-Darby canine kidney cells. Short term prevention of glycan-calnexin interactions by castanospermine slightly increases ER retention of β(1), suggesting minor involvement of calnexin in subunit folding. However, both prolonged incubation with castanospermine and removal of N-glycosylation sites do not affect the α(1)-assembly or trafficking of β(1) but increase the amount of the β(1)-bound BiP, showing that BiP can compensate for calnexin in assisting β(1) folding. In contrast to β(1), prevention of either N-glycosylation or glycan-calnexin interactions abolishes the α(1)-assembly and export of β(2) from the ER despite increased β(2)-BiP binding. Mutations in the α(1)-interacting regions of β(1) and β(2) subunits impair α(1) assembly but do not affect folding of the β subunits tested by their sensitivity to trypsin. At the same time, these mutations increase the amount of β-bound BiP but not of β-bound calnexin and increase ER retention of both β-isoforms. BiP, therefore, prevents the ER export of folded but α(1)-unassembled β subunits. These α(1)-unassembled β subunits are degraded faster than α(1)-bound β subunits, preventing ER overload. In conclusion, folding of the β(1) and β(2) subunits is assisted predominantly by BiP and calnexin, respectively. Folded β(1) and β(2) either assemble with α(1) or bind BiP. The α(1)-bound β subunits traffic to the Golgi, whereas BiP-bound β subunits are retained and degraded in the ER.
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