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association of frameshift and splicing variants, all clustering to the C terminus of the same isoform group, with occurrence of rare left ventricular noncompaction phenotype
demonstrate that loss of giant obscurins from breast epithelial cells is associated with significantly increased phosphorylation and subsequent activation of the PI3K signaling cascade
suggest that the combination of the OBSCN p.Arg4444Trp variant and of the FLNC c.5161delG mutation, can cooperatively affect myofibril stability and increase the penetrance of muscular dystrophy in the French family
Crystal structure of the obscurin(-like-1):myomesin complex reveals a trans-complementation mechanism whereby an incomplete immunoglobulin-like domain assimilates an isoform-specific myomesin interdomain sequence.
OBSCN mutations may result in the development of a familial dilated cardiomyopathy (DCM) phenotype via haploinsufficiency. These mutations should be considered as a significant causal factor of DCM, alone or in concert with other mutations.
Gene-based association analyses shows nominal significant association with multifocal fibromuscular dysplasia for obscurin.
Findings indicate that loss of giant obscurins from breast epithelium results in disruption of the cell-cell contacts and acquisition of a mesenchymal phenotype that leads to enhanced tumorigenesis, migration and invasiveness in vitro and in vivo.
Loss of the obscurin-RhoGEF downregulates RhoA signaling and increases microtentacle formation and attachment of breast epithelial cells.
this study presents here the X-ray structure of the human titin:obscurin M10:O1 complex extending our previous work on the M10:OL1 interaction.
Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover
Nontumorigenic MCF10A breast epithelial cells stably transduced with shRNAs targeting giant obscurins exhibited increased viability ( approximately 30%) and reduced apoptosis ( approximately 20%) following exposure to the DNA-damaging agent etoposide.
OBSCN polymorphisms, in particular, highly conserved nonsynonymous Leu2116Phe variant, might contribute to aspirin hypersensitivity in asthmatics
Results describe the molecular basis for the head-to-tail interaction of the carboxyl terminus of titin and the amino-terminus of obscurin-like-1 by X-ray crystallography.
Results suggest that obscurin binds small ankyrin 1, and document a specific and direct interaction between proteins of the sarcomere and the sarcoplasmic reticulum.
The complete gene giant muscle protein obscurin was analysed. The fusion of the conventional obscurin A, containing only the GEF domain, and obscurin B, fusing into the 3' kinase exons, was experimentally confirmed and analysed.
OBSCN and C9orf65 comprise a highly accurate two-gene classifier for differentiating gastrointestinal stromal tumors and leiomyosarcomas.
Studies suggest that the obscurin abnormality may be involved in the pathogenesis of hypertrophic cardiomyopathy.
Structural and mutational studies of the binding region on small Ank1 for obscurin suggest that it consists of two ankyrin repeats with very similar structures.
Obscurin was never lacking in myofibrillar alterations, but was either preserved at the M-band level or diffusely spread over the sarcomeres.
These findings reveal a novel signaling pathway in human skeletal muscle that involves obscurin and the Rho GTPase TC10 and implicate this pathway in new sarcomere formation.
These findings implicate small obscurins in the maintenance of cardiomyocyte size and coupling.
Altogether, these results suggest that obscurin is required for the maintenance of morphological and ultrastructural integrity of skeletal muscle fibers against damage induced by intense mechanical stress and point to the diaphragm as the skeletal muscle most severely affected in obscurin-deficient mice.
obscurins are not restricted to striated muscles, but are abundantly expressed in several tissues and organs including brain, skin, kidney, liver, spleen, and lung.
the obscurin kinase domains, SK1 and SK2, are active enzymes with distinct substrate specificities.
Obscurin, by targeting ankB at the M band, contributes to the organization of subsarcolemma microtubules, localization of dystrophin at costameres, and maintenance of sarcolemmal integrity.
Results support a role of obscurin in mediating the subcellular localization of small ankyrin1 isoforms in striated muscle cells.
the Rho-GEF domain of obscurin interacts with RanBP9 and that both can interact with the N-terminal region of titin to influence the formation of the Z-disk and A/I junction
ANK2 is subject to alternative splicing that gives rise to unique polypeptides with diverse roles in cardiac function.
the organization of obscurin at different locations in the sarcomere changes during muscle development and that this might affect the interaction with ank1.5.
The obscurin gene spans more than 150 kb, contains over 80 exons and encodes a protein of approximately 720 kDa. The encoded protein contains 68 Ig domains, 2 fibronectin domains, 1 calcium/calmodulin-binding domain, 1 RhoGEF domain with an associated PH domain, and 2 serine-threonine kinase domains. This protein belongs to the family of giant sacromeric signaling proteins that includes titin and nebulin, and may have a role in the organization of myofibrils during assembly and may mediate interactions between the sarcoplasmic reticulum and myofibrils. Alternatively spliced transcript variants encoding different isoforms have been identified.
obscurin, cytoskeletal calmodulin and titin-interacting RhoGEF
, obscurin, myosin light chain kinase
, obscurin-myosin light chain kinase