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demonstrate that loss of giant obscurins from breast epithelial cells is associated with significantly increased phosphorylation and subsequent activation of the PI3K (show PIK3CA Proteins) signaling cascade
suggest that the combination of the OBSCN p.Arg4444Trp variant and of the FLNC (show FLNC Proteins) 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.
Loss of the obscurin-RhoGEF downregulates RhoA (show RHOA Proteins) 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
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.
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 (show NSDHL Proteins) muscles, but are abundantly expressed in several tissues and organs including brain, skin, kidney, liver, spleen, and lung.
the obscurin kinase domains, SK1 (show SPHK1 Proteins) and SK2 (show PAPSS2 Proteins), are active enzymes with distinct substrate specificities.
Obscurin, by targeting ankB (show ANKH Proteins) at the M band, contributes to the organization of subsarcolemma microtubules, localization of dystrophin (show DMD Proteins) at costameres, and maintenance of sarcolemmal integrity.
Results support a role of obscurin in mediating the subcellular localization of small ankyrin1 isoforms in striated (show NSDHL Proteins) muscle cells.
the Rho-GEF (show ARHGEF2 Proteins) domain of obscurin interacts with RanBP9 and that both can interact with the N-terminal region of titin (show TTN Proteins) 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