RGD Reference Report - Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C. - Rat Genome Database

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Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C.

Authors: Maiweilidan, Y  Klauza, I  Kordeli, E 
Citation: Maiweilidan Y, etal., Exp Cell Res. 2011 Apr 1;317(6):724-36. doi: 10.1016/j.yexcr.2011.01.002. Epub 2011 Jan 9.
RGD ID: 8554309
Pubmed: PMID:21223964   (View Abstract at PubMed)
DOI: DOI:10.1016/j.yexcr.2011.01.002   (Journal Full-text)

Ankyrins, the adapters of the spectrin skeleton, are involved in local accumulation and stabilization of integral proteins to the appropriate membrane domains. In striated muscle, tissue-dependent alternative splicing generates unique Ank3 gene products (ankyrins-G); they share the Obscurin/Titin-Binding-related Domain (OTBD), a muscle-specific insert of the C-terminal domain which is highly conserved among ankyrin genes, and binds obscurin and titin to Ank1 gene products. We previously proposed that OTBD sequences constitute a novel domain of protein-protein interactions which confers ankyrins with specific cellular functions in muscle. Here we searched for muscle proteins binding to ankyrin-G OTBD by yeast two hybrid assay, and we found plectin and filamin C, two organizing elements of the cytoskeleton with essential roles in myogenesis, muscle cell cytoarchitecture, and muscle disease. The three proteins coimmunoprecipitate from skeletal muscle extracts and colocalize at costameres in adult muscle fibers. During in vitro myogenesis, muscle ankyrins-G are first expressed in postmitotic myocytes undergoing fusion to myotubes. In western blots of subcellular fractions from C2C12 cells, the majority of muscle ankyrins-G appear associated with membrane compartments. Occasional but not extensive co-localization at nascent costameres suggested that ankyrin-G interactions with plectin and filamin C are not involved in costamere assembly; they would rather reinforce stability and/or modulate molecular interactions in sarcolemma microdomains by establishing novel links between muscle-specific ankyrins-G and the two costameric dystrophin-associated glycoprotein and integrin-based protein complexes. These results report the first protein-protein interactions involving the ankyrin-G OTBD domain and support the hypothesis that OTBD sequences confer ankyrins with a gain of function in vertebrates, bringing further consolidation and resilience of the linkage between sarcomeres and sarcolemma.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Ank3Ratcell surface located_inIDA PMID:21223964BHF-UCL 
Ank3Ratcostamere located_inTAS PMID:21223964BHF-UCL 
FlncRatcostamere located_inTAS PMID:21223964BHF-UCL 
PlecRatcostamere located_inTAS PMID:21223964BHF-UCL 
Ank3Ratsarcolemma located_inIDA PMID:21223964BHF-UCL 
FlncRatsarcolemma located_inIDA PMID:21223964BHF-UCL 
PlecRatsarcolemma located_inIDA PMID:21223964BHF-UCL 
FlncRatsarcoplasm located_inIDA PMID:21223964BHF-UCL 
PlecRatsarcoplasm located_inIDA PMID:21223964BHF-UCL 

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Ank3  (ankyrin 3)
Flnc  (filamin C)
Plec  (plectin)


Additional Information