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  1. Article ; Online: Cytoskeleton and CFTR.

    Edelman, Aleksander

    The international journal of biochemistry & cell biology

    2014  Volume 52, Page(s) 68–72

    Abstract: Cystic Fibrosis Transmembrane conductance Regulator, CFTR, is a membrane protein expressed in epithelia. A protein kinase A (PKA)-regulated Cl(-) channel, it is a rate-limiting factor in fluid transport. Mutations in CFTR are responsible for cystic ... ...

    Abstract Cystic Fibrosis Transmembrane conductance Regulator, CFTR, is a membrane protein expressed in epithelia. A protein kinase A (PKA)-regulated Cl(-) channel, it is a rate-limiting factor in fluid transport. Mutations in CFTR are responsible for cystic fibrosis, CF, an autosomal recessive disease. The most frequent mutation is deletion of phenylalanine at position 508, ΔF508. The regulation of trafficking and degradation of CFTR/ΔF508CFTR as well as its function(s) is a complex process which involves a number of proteins including chaperones and adaptors. It is now known that cytoskeletal proteins, previously considered only as structural proteins, are also important factors in the regulation of cellular processes and functions. The aim of the present review is to focus on how microfilaments, microtubules and intermediary filaments form a dynamic interactome with CFTR to participate in the regulation of CFTR-dependent transepithelial ion transport, CFTR trafficking and degradation.
    MeSH term(s) Animals ; Cystic Fibrosis/genetics ; Cystic Fibrosis/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Cytoskeleton/metabolism ; Humans
    Chemical Substances Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2014-07
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 1228429-4
    ISSN 1878-5875 ; 1357-2725
    ISSN (online) 1878-5875
    ISSN 1357-2725
    DOI 10.1016/j.biocel.2014.03.018
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  2. Article: Cytoskeleton and CFTR

    Edelman, Aleksander

    international journal of biochemistry & cell biology. 2014 July, v. 52

    2014  

    Abstract: Cystic Fibrosis Transmembrane conductance Regulator, CFTR, is a membrane protein expressed in epithelia. A protein kinase A (PKA)-regulated Cl− channel, it is a rate-limiting factor in fluid transport. Mutations in CFTR are responsible for cystic ... ...

    Abstract Cystic Fibrosis Transmembrane conductance Regulator, CFTR, is a membrane protein expressed in epithelia. A protein kinase A (PKA)-regulated Cl− channel, it is a rate-limiting factor in fluid transport. Mutations in CFTR are responsible for cystic fibrosis, CF, an autosomal recessive disease. The most frequent mutation is deletion of phenylalanine at position 508, ΔF508. The regulation of trafficking and degradation of CFTR/ΔF508CFTR as well as its function(s) is a complex process which involves a number of proteins including chaperones and adaptors. It is now known that cytoskeletal proteins, previously considered only as structural proteins, are also important factors in the regulation of cellular processes and functions. The aim of the present review is to focus on how microfilaments, microtubules and intermediary filaments form a dynamic interactome with CFTR to participate in the regulation of CFTR-dependent transepithelial ion transport, CFTR trafficking and degradation.This article is part of a Directed Issue entitled: Cystic Fibrosis: From o-mics to cell biology, physiology, and therapeutic advances.
    Keywords cAMP-dependent protein kinase ; chlorides ; cystic fibrosis ; cystic fibrosis transmembrane conductance regulator ; cytoskeletal proteins ; epithelium ; microfilaments ; microtubules ; mutation ; phenylalanine ; physiology ; structural proteins ; therapeutics
    Language English
    Dates of publication 2014-07
    Size p. 68-72.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 1228429-4
    ISSN 1878-5875 ; 1357-2725
    ISSN (online) 1878-5875
    ISSN 1357-2725
    DOI 10.1016/j.biocel.2014.03.018
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  3. Article ; Online: Cystic fibrosis, a multi-systemic mucosal disease: 25 years after the discovery of CFTR.

    Edelman, Aleksander / Sallenave, Jean-Michel

    The international journal of biochemistry & cell biology

    2014  Volume 52, Page(s) 2–4

    MeSH term(s) Animals ; Cystic Fibrosis/genetics ; Cystic Fibrosis/physiopathology ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Humans
    Chemical Substances Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2014-07
    Publishing country Netherlands
    Document type Editorial
    ZDB-ID 1228429-4
    ISSN 1878-5875 ; 1357-2725
    ISSN (online) 1878-5875
    ISSN 1357-2725
    DOI 10.1016/j.biocel.2014.04.006
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  4. Article: Physiopathologie à l'ère de la protéomique contemporaine.

    Edelman, Aleksander

    Medecine sciences : M/S

    2005  Volume 21, Issue 8-9, Page(s) 675–678

    Title translation Pathophysiology in the era of contemporary proteomics.
    MeSH term(s) Animals ; Gene Expression Regulation ; Humans ; Pathology/trends ; Physiology/trends ; Proteins/genetics ; Proteomics/methods
    Chemical Substances Proteins
    Language French
    Publishing date 2005-08
    Publishing country France
    Document type Comment ; Editorial
    ZDB-ID 632733-3
    ISSN 1958-5381 ; 0767-0974
    ISSN (online) 1958-5381
    ISSN 0767-0974
    DOI 10.1051/medsci/2005218-9675
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  5. Article: Emerging Therapeutic Approaches for Cystic Fibrosis. From Gene Editing to Personalized Medicine.

    Pranke, Iwona / Golec, Anita / Hinzpeter, Alexandre / Edelman, Aleksander / Sermet-Gaudelus, Isabelle

    Frontiers in pharmacology

    2019  Volume 10, Page(s) 121

    Abstract: An improved understanding of the cystic fibrosis (CF) transmembrane conductance regulator (CFTR) protein structure and the consequences ... ...

    Abstract An improved understanding of the cystic fibrosis (CF) transmembrane conductance regulator (CFTR) protein structure and the consequences of
    Language English
    Publishing date 2019-02-27
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2587355-6
    ISSN 1663-9812
    ISSN 1663-9812
    DOI 10.3389/fphar.2019.00121
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  6. Article ; Online: Pharmacological chaperone-rescued cystic fibrosis CFTR-F508del mutant overcomes PRAF2-gated access to endoplasmic reticulum exit sites

    Saha, Kusumika / Chevalier, Benoit / Doly, Stéphane / Baatallah, Nesrine / Guilbert, Thomas / Pranke, Iwona / Scott, Mark G. H. / Enslen, Hervé / Guerrera, Chiara / Chuon, Cérina / Edelman, Aleksander / Sermet-Gaudelus, Isabelle / Hinzpeter, Alexandre / Marullo, Stefano

    Cell. Mol. Life Sci.. 2022 Oct., v. 79, no. 10 p.530-530

    2022  

    Abstract: The endoplasmic reticulum exit of some polytopic plasma membrane proteins (PMPs) is controlled by arginin-based retention motifs. PRAF2, a gatekeeper which recognizes these motifs, was shown to retain the GABAB-receptor GB1 subunit in the ER. We report ... ...

    Abstract The endoplasmic reticulum exit of some polytopic plasma membrane proteins (PMPs) is controlled by arginin-based retention motifs. PRAF2, a gatekeeper which recognizes these motifs, was shown to retain the GABAB-receptor GB1 subunit in the ER. We report that PRAF2 can interact on a stoichiometric basis with both wild type and mutant F508del Cystic Fibrosis (CF) Transmembrane Conductance Regulator (CFTR), preventing the access of newly synthesized cargo to ER exit sites. Because of its lower abundance, compared to wild-type CFTR, CFTR-F508del recruitment into COPII vesicles is suppressed by the ER-resident PRAF2. We also demonstrate that some pharmacological chaperones that efficiently rescue CFTR-F508del loss of function in CF patients target CFTR-F508del retention by PRAF2 operating with various mechanisms. Our findings open new therapeutic perspectives for diseases caused by the impaired cell surface trafficking of mutant PMPs, which contain RXR-based retention motifs that might be recognized by PRAF2.
    Keywords cystic fibrosis ; endoplasmic reticulum ; mutants ; plasma membrane ; stoichiometry ; therapeutics
    Language English
    Dates of publication 2022-10
    Size p. 530.
    Publishing place Springer International Publishing
    Document type Article ; Online
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-022-04554-1
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  7. Article: Putting bicarbonate on the spot: pharmacological insights for CFTR correction in the airway epithelium.

    Zajac, Miroslaw / Lepissier, Agathe / Dréano, Elise / Chevalier, Benoit / Hatton, Aurélie / Kelly-Aubert, Mairead / Guidone, Daniela / Planelles, Gabrielle / Edelman, Aleksander / Girodon, Emmanuelle / Hinzpeter, Alexandre / Crambert, Gilles / Pranke, Iwona / Galietta, Luis J V / Sermet-Gaudelus, Isabelle

    Frontiers in pharmacology

    2023  Volume 14, Page(s) 1293578

    Abstract: Introduction: ...

    Abstract Introduction:
    Language English
    Publishing date 2023-12-11
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587355-6
    ISSN 1663-9812
    ISSN 1663-9812
    DOI 10.3389/fphar.2023.1293578
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  8. Article ; Online: A small molecule chaperone rescues keratin-8 mediated trafficking of misfolded podocin to correct genetic Nephrotic Syndrome.

    Kuzmuk, Valeryia / Pranke, Iwona / Rollason, Ruth / Butler, Matthew / Ding, Wen Y / Beesley, Matthew / Waters, Aoife M / Coward, Richard J / Sessions, Richard / Tuffin, Jack / Foster, Rebecca R / Mollet, Géraldine / Antignac, Corinne / Edelman, Aleksander / Welsh, Gavin I / Saleem, Moin A

    Kidney international

    2023  Volume 105, Issue 4, Page(s) 744–758

    Abstract: Podocin is a key membrane scaffolding protein of the kidney podocyte essential for intact glomerular filtration. Mutations in NPHS2, the podocin-encoding gene, represent the commonest form of inherited nephrotic syndrome (NS), with early, intractable ... ...

    Abstract Podocin is a key membrane scaffolding protein of the kidney podocyte essential for intact glomerular filtration. Mutations in NPHS2, the podocin-encoding gene, represent the commonest form of inherited nephrotic syndrome (NS), with early, intractable kidney failure. The most frequent podocin gene mutation in European children is R138Q, causing retention of the misfolded protein in the endoplasmic reticulum. Here, we provide evidence that podocin R138Q (but not wild-type podocin) complexes with the intermediate filament protein keratin 8 (K8) thereby preventing its correct trafficking to the plasma membrane. We have also identified a small molecule (c407), a compound that corrects the Cystic Fibrosis Transmembrane Conductance Regulator protein defect, that interrupts this complex and rescues mutant protein mistrafficking. This results in both the correct localization of podocin at the plasma membrane and functional rescue in both human patient R138Q mutant podocyte cell lines, and in a mouse inducible knock-in model of the R138Q mutation. Importantly, complete rescue of proteinuria and histological changes was seen when c407 was administered both via osmotic minipumps or delivered orally prior to induction of disease or crucially via osmotic minipump two weeks after disease induction. Thus, our data constitute a therapeutic option for patients with NS bearing a podocin mutation, with implications for other misfolding protein disorders. Further studies are necessary to confirm our findings.
    MeSH term(s) Animals ; Child ; Humans ; Mice ; Intracellular Signaling Peptides and Proteins/genetics ; Keratin-8/genetics ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Molecular Chaperones/genetics ; Mutation ; Nephrotic Syndrome/drug therapy ; Nephrotic Syndrome/genetics ; Nephrotic Syndrome/pathology
    Chemical Substances Intracellular Signaling Peptides and Proteins ; Keratin-8 ; Membrane Proteins ; Molecular Chaperones ; NPHS2 protein ; KRT8 protein, human
    Language English
    Publishing date 2023-11-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 120573-0
    ISSN 1523-1755 ; 0085-2538
    ISSN (online) 1523-1755
    ISSN 0085-2538
    DOI 10.1016/j.kint.2023.11.006
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 797: Show issues Location:
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  9. Article ; Online: Acting on the CFTR Membrane-Spanning Domains Interface Rescues Some Misfolded Mutants.

    Baatallah, Nesrine / Elbahnsi, Ahmad / Chevalier, Benoit / Castanier, Solène / Mornon, Jean-Paul / Pranke, Iwona / Edelman, Aleksander / Sermet-Gaudelus, Isabelle / Callebaut, Isabelle / Hinzpeter, Alexandre

    International journal of molecular sciences

    2022  Volume 23, Issue 24

    Abstract: ABC transporters are large membrane proteins sharing a complex architecture, which comprises two nucleotide-binding domains (NBDs) and two membrane-spanning domains (MSDs). These domains are susceptible to mutations affecting their folding and assembly. ... ...

    Abstract ABC transporters are large membrane proteins sharing a complex architecture, which comprises two nucleotide-binding domains (NBDs) and two membrane-spanning domains (MSDs). These domains are susceptible to mutations affecting their folding and assembly. In the CFTR (ABCC7) protein, a groove has been highlighted in the MSD1 at the level of the membrane inner leaflet, containing both multiple mutations affecting folding and a binding site for pharmaco-chaperones that stabilize this region. This groove is also present in ABCB proteins, however it is covered by a short elbow helix, while in ABCC proteins it remains unprotected, due to a lower position of the elbow helix in the presence of the ABCC-specific lasso motif. Here, we identified a MSD1 second-site mutation located in the vicinity of the CFTR MSD1 groove that partially rescued the folding defect of cystic fibrosis causing mutations located within MSD1, while having no effect on the most frequent mutation, F508del, located within NBD1. A model of the mutated protein 3D structure suggests additional interaction between MSD1 and MSD2, strengthening the assembly at the level of the MSD intracellular loops. Altogether, these results provide insightful information in understanding key features of the folding and function of the CFTR protein in particular, and more generally, of type IV ABC transporters.
    Language English
    Publishing date 2022-12-19
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms232416225
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  10. Article ; Online: Differential CFTR-Interactome Proximity Labeling Procedures Identify Enrichment in Multiple SLC Transporters.

    Chevalier, Benoît / Baatallah, Nesrine / Najm, Matthieu / Castanier, Solène / Jung, Vincent / Pranke, Iwona / Golec, Anita / Stoven, Véronique / Marullo, Stefano / Antigny, Fabrice / Guerrera, Ida Chiara / Sermet-Gaudelus, Isabelle / Edelman, Aleksander / Hinzpeter, Alexandre

    International journal of molecular sciences

    2022  Volume 23, Issue 16

    Abstract: Proteins interacting with CFTR and its mutants have been intensively studied using different experimental approaches. These studies provided information on the cellular processes leading to proper protein folding, routing to the plasma membrane, ... ...

    Abstract Proteins interacting with CFTR and its mutants have been intensively studied using different experimental approaches. These studies provided information on the cellular processes leading to proper protein folding, routing to the plasma membrane, recycling, activation and degradation. Recently, new approaches have been developed based on the proximity labeling of protein partners or proteins in close vicinity and their subsequent identification by mass spectrometry. In this study, we evaluated TurboID- and APEX2-based proximity labeling of WT CFTR and compared the obtained data to those reported in databases. The CFTR-WT interactome was then compared to that of two CFTR (G551D and W1282X) mutants and the structurally unrelated potassium channel KCNK3. The two proximity labeling approaches identified both known and additional CFTR protein partners, including multiple SLC transporters. Proximity labeling approaches provided a more comprehensive picture of the CFTR interactome and improved our knowledge of the CFTR environment.
    MeSH term(s) Cell Membrane/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Mass Spectrometry ; Mutation ; Protein Folding
    Chemical Substances Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2022-08-11
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23168937
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