Classification and rescue of ROMK mutations underlying hyperprostaglandin E syndrome/antenatal Bartter syndrome

Peters, Melanie; Ermert, Saskia Christine; Jeck, Nikola; Derst, Christian; Pechmann, Ulla; Weber, Stefanie; Schlingmann, Karl Peter; Seyberth, H. W.; Waldegger, Siegfried; Konrad, Martin

doi:10.1046/j.1523-1755.2003.00153.x

Cited by 71 publications

(68 citation statements)

References 38 publications

(72 reference statements)

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“…When examined under steady-state conditions in mammalian cells, ROMK primarily resides in the ER (35,41). Similarly, we found that the majority of ROMK1S44D+K80M co-migrated with the ER-resident protein Sec61 when lysates from a wild-type yeast strain isogenic to trk1Δtrk2Δ and its derivatives (BY4742) were subjected to subcellular fractionation by sucrose gradient sedimentation analysis ( Figure 1D).…”

Section: Identification Of a Romk Variant Suitable Formentioning

confidence: 91%

“…Interestingly, individuals heterozygous for a type II Bartter mutant allele exhibit resistance to hypertension, most likely because of decreased NKCC2-mediated reabsorption of sodium (40). Of the >50 identified Bartter syndrome-associated mutations in ROMK, many appear to affect ROMK trafficking or post translational modification when ectopically expressed in Xenopus laevis oocytes (41). To date, therapies for Bartter syndrome are not curative and patients require lifelong multi-drug treatments and potassium supplementation.…”

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confidence: 99%

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The endosomal trafficking factors CORVET and ESCRT suppress plasma membrane residence of the renal outer medullary potassium channel (ROMK)

Mackie

Kim

Subramanya

et al. 2018

Journal of Biological Chemistry

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Section: Identification Of a Romk Variant Suitable Formentioning

confidence: 91%

mentioning

confidence: 99%

The endosomal trafficking factors CORVET and ESCRT suppress plasma membrane residence of the renal outer medullary potassium channel (ROMK)

Mackie

Kim

Subramanya

et al. 2018

Journal of Biological Chemistry

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“…AQP2 mutations that are responsible for autosomal recessive NDI are characterized by misrouting of the misfolded mutant proteins and are trapped in the endoplasmic reticulum (53). Mutants that encode other renal membrane proteins that are responsible for Gitelman syndrome (54), Bartter syndrome (55,56), and cystinuria (57) are also retained in the endoplasmic reticulum.…”

Section: X-linked Ndi (Omim 304800) As a Results Of Mutations In Avpr2mentioning

confidence: 99%

Molecular Biology of Hereditary Diabetes Insipidus

Fujiwara

Bichet

2005

Journal of the American Society of Nephrology

223

150

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A nyone who passes large volumes of urine might be said to be experiencing diabetes insipidus. Years ago, the initial distinction made by physicians in evaluating patients with polyuria was whether their urine was sweet (diabetes mellitus) or not (diabetes insipidus) (1). Diabetes insipidus is a disorder characterized by the excretion of abnormally large volumes (Ͼ30 ml/kg body wt/d for adults) of dilute urine (Ͻ250 mmol/kg). This definition excludes osmotic diuresis, which occurs when excess solute is being excreted, for example, glucose in the polyuria of diabetes mellitus. Four basic defects can be involved: (1) deficient secretion of the antidiuretic hormone arginine vasopressin (AVP), which is the most common defect and is referred to as neurohypophyseal (also known to as neurogenic, central, or hypothalamic) diabetes insipidus; (2) renal insensitivity to the antidiuretic effect of AVP, which is known as nephrogenic diabetes insipidus (NDI); (3) excessive water intake that can result in polyuria, which is referred to as primary polydipsia; and (4) increased metabolism of vasopressin during pregnancy, which is referred to as gestational diabetes insipidus. The hereditary forms of diabetes insipidus account for Ͻ10% of the cases of diabetes insipidus seen in clinical practice. The purpose of this review is to examine recent developments in the understanding and molecular biology of the hereditary forms of diabetes insipidus. Here we use the gene symbols approved by the HUGO Gene Nomenclature Committee (http://www.gene.ucl.ac.uk/nomenclature) and provide OMIM entry numbers (2). Not included in this review are acquired forms of NDI; for further information, see references 3-5. Genes Involved in "Pure" Diabetes Insipidus AVPThe regulation of the release of AVP from the posterior pituitary is primarily dependent, under normal circumstances, on tonicity information relayed by osmoreceptor cells in the anterior hypothalamus (6). AVP and its corresponding carrier, neurophysin II, are synthesized as a composite precursor by the magnocellular neurons of the supraoptic and paraventricular nuclei of the hypothalamus (for review, see 7). The precursor is packaged into neurosecretory granules and transported axonally in the stalk of the posterior pituitary. En route to the neurohypophysis, the precursor is processed into the active hormone. Prepro-vasopressin has 164 amino acids and is encoded by the 2.5-kb AVP gene located in chromosome region 20p13 (8,9). The AVP gene (coding for AVP and neurophysin II) and the OXT gene (coding for oxytocin and neurophysin I) are located in the same chromosome region, at a very short distance from each other (12 kb in humans) in head-to-head orientation. Data from transgenic mouse studies indicate that the intergenic region between the OXT and the AVP genes contains the critical enhancer sites for cell-specific expression in the magnocellular neurons (7). It is phylogenetically interesting to note that cis and trans components of this specific cellular expression have been conserved bet...

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“…Mutation of any of these six residues alters the pH i sensitivity of Kir1.1 (645). R311W and A177T, which are found to cause Bartter's syndrome, change pK a of Kir1.1 (ϳ6.5) to 9.2 and 7.8 in Kir1.1, respectively, which results in dysfunction of the channel in physiological pH i range (617,645,696) (see also sect. VA6 and Table 2).…”

Section: Pore Structure and Functionmentioning

confidence: 99%

Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles

Hibino

Inanobe

Furutani

et al. 2010

Physiological Reviews

1,296

1,496

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Inwardly rectifying K+(Kir) channels allow K+to move more easily into rather than out of the cell. They have diverse physiological functions depending on their type and their location. There are seven Kir channel subfamilies that can be classified into four functional groups: classical Kir channels (Kir2.x) are constitutively active, G protein-gated Kir channels (Kir3.x) are regulated by G protein-coupled receptors, ATP-sensitive K+channels (Kir6.x) are tightly linked to cellular metabolism, and K+transport channels (Kir1.x, Kir4.x, Kir5.x, and Kir7.x). Inward rectification results from pore block by intracellular substances such as Mg2+and polyamines. Kir channel activity can be modulated by ions, phospholipids, and binding proteins. The basic building block of a Kir channel is made up of two transmembrane helices with cytoplasmic NH2and COOH termini and an extracellular loop which folds back to form the pore-lining ion selectivity filter. In vivo, functional Kir channels are composed of four such subunits which are either homo- or heterotetramers. Gene targeting and genetic analysis have linked Kir channel dysfunction to diverse pathologies. The crystal structure of different Kir channels is opening the way to understanding the structure-function relationships of this simple but diverse ion channel family.

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Classification and rescue of ROMK mutations underlying hyperprostaglandin E syndrome/antenatal Bartter syndrome

Cited by 71 publications

References 38 publications

The endosomal trafficking factors CORVET and ESCRT suppress plasma membrane residence of the renal outer medullary potassium channel (ROMK)

The endosomal trafficking factors CORVET and ESCRT suppress plasma membrane residence of the renal outer medullary potassium channel (ROMK)

Molecular Biology of Hereditary Diabetes Insipidus

Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles

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