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Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Poparic, I; Schreibmayer, W; Schoser, B; Desoye, G; Gorischek, A; Miedl, H; Hochmeister, S; Binder, J; Quasthoff, S; Wagner, K; Windpassinger, C; Malle, E.
Four and a half LIM protein 1C (FHL1C): a binding partner for voltage-gated potassium channel K(v1.5).
PLOS ONE. 2011; 6(10): e26524-e26524.
Doi: 10.1371/journal.pone.0026524
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- Führende Autor*innen der Med Uni Graz
- Poparic Ivana
- Windpassinger Christian
- Co-Autor*innen der Med Uni Graz
- Binder Josepha Stephanie
- Desoye Gernot
- Gorischek Astrid
- Hochmeister Sonja
- Malle Ernst
- Miedl Heidi
- Quasthoff Stefan
- Schreibmayer Wolfgang
- Wagner Klaus
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- Abstract:
- Four-and-a-half LIM domain protein 1 isoform A (FHL1A) is predominantly expressed in skeletal and cardiac muscle. Mutations in the FHL1 gene are causative for several types of hereditary myopathies including X-linked myopathy with postural muscle atrophy (XMPMA). We here studied myoblasts from XMPMA patients. We found that functional FHL1A protein is completely absent in patient myoblasts. In parallel, expression of FHL1C is either unaffected or increased. Furthermore, a decreased proliferation rate of XMPMA myoblasts compared to controls was observed but an increased number of XMPMA myoblasts was found in the G(0)/G(1) phase. Furthermore, low expression of K(v1.5), a voltage-gated potassium channel known to alter myoblast proliferation during the G(1) phase and to control repolarization of action potential, was detected. In order to substantiate a possible relation between K(v1.5) and FHL1C, a pull-down assay was performed. A physical and direct interaction of both proteins was observed in vitro. In addition, confocal microscopy revealed substantial colocalization of FHL1C and K(v1.5) within atrial cells, supporting a possible interaction between both proteins in vivo. Two-electrode voltage clamp experiments demonstrated that coexpression of K(v1.5) with FHL1C in Xenopus laevis oocytes markedly reduced K(+) currents when compared to oocytes expressing K(v1.5) only. We here present the first evidence on a biological relevance of FHL1C.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Blotting, Western -
- Case-Control Studies -
- Cell Cycle -
- Cell Line -
- Cell Proliferation -
- Genetic Diseases, X-Linked - metabolism Genetic Diseases, X-Linked - pathology
- Humans -
- Intracellular Signaling Peptides and Proteins - genetics Intracellular Signaling Peptides and Proteins - metabolism
- Ion Channel Gating -
- Kinetics -
- Kv1.5 Potassium Channel - genetics Kv1.5 Potassium Channel - metabolism
- LIM Domain Proteins - genetics LIM Domain Proteins - metabolism
- Male -
- Mice -
- Muscle Proteins - genetics Muscle Proteins - metabolism
- Muscular Atrophy - metabolism Muscular Atrophy - pathology
- Mutant Proteins - metabolism
- Myoblasts - metabolism Myoblasts - pathology
- Protein Binding -
- Protein Isoforms - genetics Protein Isoforms - metabolism
- Protein Transport -
- Reverse Transcriptase Polymerase Chain Reaction -
- Subcellular Fractions - metabolism
- Xenopus -
- Xenopus laevis -