Different obscurin isoforms localize to distinct sites at sarcomeres

Bowman, Amber L.; Kontrogianni‐Konstantopoulos, Aikaterini; Hirsch, Sara S.; Geisler, Stefanie; González‐Serratos, Hugo; Russell, Mark W.; Bloch, Robert J.

doi:10.1016/j.febslet.2007.03.011

Cited by 51 publications

(80 citation statements)

References 22 publications

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“…S1A,Bf,g). This result confirms previous findings (Bowman et al, 2007;Fukuzawa et al, 2005) that the obscurin kinase region might be independently expressed as KIAA1639 (Fig. 1D).…”

Section: Generation Of the Obscurin Knockoutsupporting

confidence: 82%

“…Obsc has been found to localize to several subcellular compartments within cross-striated muscles cells, notably the Zdisc, A-I junction as well as the M-band of the sarcomere (Carlsson et al, 2008). Moreover, the subcellular localization of obscurin was attributed to different Obsc isoforms (Bowman et al, 2007). According to our western blot analysis (Fig.…”

Section: Obscurin Is Expressed In Cross-striated Musclesmentioning

confidence: 93%

“…Obscurin (Obsc) was first described as a binding partner for Zdisc domains Z9 and Z10 of titin, but later was shown to have a more diverse localization within the sarcomere (Bang et al, 2001;Bowman et al, 2007;Carlsson et al, 2008;Young et al, 2001). Obsc belongs, like titin, to the class of giant proteins with a domain layout that is largely comprised of immunoglobulin-like (Ig) and fibronectin type III (Fn) domains.…”

Section: Introductionmentioning

confidence: 99%

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Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum

Lange

Ouyang

Meyer

et al. 2009

Journal of Cell Science

120

165

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The giant protein obscurin is thought to link the sarcomere with the sarcoplasmic reticulum (SR). The N-terminus of obscurin interacts with the M-band proteins titin and myomesin, whereas the C-terminus mediates interactions with ankyrin proteins. Here, we investigate the importance of obscurin for SR architecture and organization. Lack of obscurin in crossstriated muscles leads to changes in longitudinal SR architecture and disruption of small ankyrin-1.5 (sAnk1.5) expression and localization. Changes in SR architecture in obscurin knockout mice are also associated with alterations in several SR or SRassociated proteins, such as ankyrin-2 and β-spectrin. Finally, obscurin knockout mice display centralized nuclei in skeletal muscles as a sign of mild myopathy, but have normal sarcomeric structure and preserved muscle function. Supplementary material available online at

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“…S1A,Bf,g). This result confirms previous findings (Bowman et al, 2007;Fukuzawa et al, 2005) that the obscurin kinase region might be independently expressed as KIAA1639 (Fig. 1D).…”

Section: Generation Of the Obscurin Knockoutsupporting

confidence: 82%

Section: Obscurin Is Expressed In Cross-striated Musclesmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum

Lange

Ouyang

Meyer

et al. 2009

Journal of Cell Science

120

165

View full text Add to dashboard Cite

show abstract

“…Epitopes mapping to the NH 2 -and COOH-termini of giant obscurins localize to the Z-disc, while an epitope to the SK2 region of obscurin-B maps to the outer periphery of the Z-disc (Bowman et al 2007), supporting the notion that multiple obscurin isoforms localize to the Z-disc region of the sarcomere (Table 1; Fig. 2).…”

Section: Obscurins At the Z-discsupporting

confidence: 52%

“…2) (Bowman et al 2007;Fukuzawa et al 2008;Kontrogianni-Konstantopoulos et al 2006;Shriver et al 2015). The specific isoforms of obscurin expressed at these locations is not well established.…”

Section: Diversity Of the Subcellular Distribution Of Obscurinsmentioning

confidence: 99%

Obscure functions: the location–function relationship of obscurins

2017

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The obscurin family of polypeptides is essential for normal striated muscle function and contributes to the pathogenesis of fatal diseases, including cardiomyopathies and cancers. The single mammalian obscurin gene, OBSCN, gives rise to giant (∼800 kDa) and smaller (∼40-500 kDa) proteins that are composed of tandem adhesion and signaling motifs. Mammalian obscurin proteins are expressed in a variety of cell types, including striated muscles, and localize to distinct subcellular compartments where they contribute to diverse cellular processes. Obscurin homologs in Caenorhabditis elegans and Drosophila possess a similar domain architecture and are also expressed in striated muscles. The long sought after question, "what does obscurin do?" is complex and cannot be addressed without taking into consideration the subcellular distribution of these proteins and local isoform concentration. Herein, we present an overview of the functions of obscurins and begin to define the intricate relationship between their subcellular distributions and functions in striated muscles.

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Myofilaments: Movers and Rulers of the Sarcomere

Lin

Song

Sadayappan

2017

Comprehensive Physiology

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Striated cardiac and skeletal muscles play very different roles in the body, but they are similar at the molecular level. In particular, contraction, regardless of the type of muscle, is a precise and complex process involving the integral protein myofilaments and their associated regulatory components. The smallest functional unit of muscle contraction is the sarcomere. Within the sarcomere can be found a sophisticated ensemble of proteins associated with the thick filaments (myosin, myosin binding protein-C, titin, and obscurin) and thin myofilaments (actin, troponin, tropomyosin, nebulin, and nebulette). These parallel thick and thin filaments slide across one another, pulling the two ends of the sarcomere together to regulate contraction. More specifically, the regulation of both timing and force of contraction is accomplished through an intricate network of intra- and interfilament interactions belonging to each myofilament. This review introduces the sarcomere proteins involved in striated muscle contraction and places greater emphasis on the more recently identified and less well-characterized myofilaments: cardiac myosin binding protein-C, titin, nebulin, and obscurin. © 2017 American Physiological Society. Compr Physiol 7:675-692, 2017.

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Different obscurin isoforms localize to distinct sites at sarcomeres

Cited by 51 publications

References 22 publications

Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum

Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum

Obscure functions: the location–function relationship of obscurins

Myofilaments: Movers and Rulers of the Sarcomere

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