Topology of interaction between titin and myosin thick filaments

Kellermayer, Miklós; Sziklai, Dominik; Papp, Zsombor; Decker, Brennan; Lakatos, Eszter; Mártonfalvi, Zsolt

doi:10.1016/j.jsb.2018.05.001

Cited by 5 publications

(4 citation statements)

References 31 publications

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“…Moreover, age-related loss of NO-synthase in the skeletal muscles was reported to decrease calpain S-nitrosylation, thereby leading to increased myofibril degradation and sarcopenia (Samengo et al, 2012). In addition, the proteolytic susceptibility of titin, the giant elastic protein present in vertebrate striated muscles (Tskhovrebova and Trinick, 2017; Herzog, 2018; Kellermayer et al, 2018; Linke, 2018), has been reported to be affected by titin phosphorylation (Gritsyna et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Effect of L-Arginine on Titin Expression in Rat Soleus Muscle After Hindlimb Unloading

et al. 2019

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Nitric oxide (NO), produced by NO-synthases via L-arginine oxidation, is an essential trigger for signaling processes involved in structural and metabolic changes in muscle fibers. Recently, it was shown that L-arginine administration prevented the decrease in levels of the muscle cytoskeletal proteins, desmin and dystrophin, in rat soleus muscle after 14 days of hindlimb unloading. Therefore, in this study, we investigated the effect of L-arginine administration on the degree of atrophy changes in the rat soleus muscles under unloading conditions, and on the content, gene expression, and phosphorylation level of titin, the giant protein of striated muscles, able to form a third type of myofilaments—elastic filaments. A 7-day gravitational unloading [hindlimb suspension (HS) group] resulted in a decrease in the soleus weight:body weight ratio (by 31.8%, p < 0.05), indicating muscle atrophy development. The content of intact titin (T1) decreased (by 22.4%, p < 0.05) and the content of proteolytic fragments of titin (T2) increased (by 66.7%, p < 0.05) in the soleus muscle of HS rats, compared to control rats. The titin gene expression and phosphorylation level of titin between these two groups were not significantly different. L-Arginine administration under 7-day gravitational unloading decreased the degree of atrophy changes and also prevented the decrease in levels of T1 in the soleus muscle as compared to HS group. Furthermore, L-arginine administration under unloading resulted in increased titin mRNA level (by 76%, p < 0.05) and decreased phosphorylation level of T2 (by 28%, p < 0.05), compared to those in the HS group. These results suggest that administration of L-arginine, the NO precursor, under unloading decreased the degree of atrophy changes, increased gene expression of titin and prevented the decrease in levels of T1 in the rat soleus muscle. The results can be used to search for approaches to reduce the development of negative changes caused by gravitational unloading in the muscle.

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Section: Introductionmentioning

confidence: 99%

Effect of L-Arginine on Titin Expression in Rat Soleus Muscle After Hindlimb Unloading

et al. 2019

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“…The subunit structure is possibly related to the appearance of M-lines within the M-band [18,19]. As the histogram of the number of titin molecules has local modes at 6 and 12 (Figure 1d) [47,51], the M-complex is most likely a structural unit that reflects the transversal organization of titin molecules dictated by the myosin thick filament, even though myosin molecules, which have a characteristic two-headed appearance in AFM images [47], were totally absent from the sample. The complete absence of myosin is likely due to efficient chromatography purification.…”

Section: Topographical Structure Stability and Organization Of The Ti...mentioning

confidence: 95%

“…Samples were prepared for AFM imaging as described previously [47]. Briefly, protein samples (at a concentration between 0.3-0.5 mg/mL) were diluted (100×) in chromatography buffer, then 20 µL was pipetted onto freshly cleaved mica and incubated for 1 min.…”

Section: Titin Sample Preparation For Afmmentioning

confidence: 99%

“…Considering that the C-terminus of titin extends into the M-band of the muscle sarcomere [17] where titin interacts with a number of proteins such as myomesin [21], M-line protein [21], myomesin-3 [49], and obscurin [50], we hereby refer to the globular head-like structure of titin as the M-complex, even though in the present work, we did not directly quantify the proportion of the additional protein components. The M-complex serves as a focal point of interaction in head-to-head oligomers of titin (Figure 1b) [17,47,51,52]. In a three-dimensional space, the M-band is a thick, two-dimensional plate traversing the cross-section of the myofibril and positioned in the center of each sarcomere [53].…”

Section: Topographical Structure Stability and Organization Of The Ti...mentioning

confidence: 99%

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Nanosurgical Manipulation of Titin and Its M-Complex

et al. 2022

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Titin is a multifunctional filamentous protein anchored in the M-band, a hexagonally organized supramolecular lattice in the middle of the muscle sarcomere. Functionally, the M-band is a framework that cross-links myosin thick filaments, organizes associated proteins, and maintains sarcomeric symmetry via its structural and putative mechanical properties. Part of the M-band appears at the C-terminal end of isolated titin molecules in the form of a globular head, named here the “M-complex”, which also serves as the point of head-to-head attachment of titin. We used high-resolution atomic force microscopy and nanosurgical manipulation to investigate the topographical and internal structure and local mechanical properties of the M-complex and its associated titin molecules. We find that the M-complex is a stable structure that corresponds to the transverse unit of the M-band organized around the myosin thick filament. M-complexes may be interlinked into an M-complex array that reflects the local structural and mechanical status of the transversal M-band lattice. Local segments of titin and the M-complex could be nanosurgically manipulated to achieve extension and domain unfolding. Long threads could be pulled out of the M-complex, suggesting that it is a compact supramolecular reservoir of extensible filaments. Nanosurgery evoked an unexpected volume increment in the M-complex, which may be related to its function as a mechanical spacer. The M-complex thus displays both elastic and plastic properties which support the idea that the M-band may be involved in mechanical functions within the muscle sarcomere.

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High-Speed Atomic Force Microscopy to Study Myosin Motility

Kodera

Ando

2020

Advances in Experimental Medicine and Biology

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Topology of interaction between titin and myosin thick filaments

Cited by 5 publications

References 31 publications

Effect of L-Arginine on Titin Expression in Rat Soleus Muscle After Hindlimb Unloading

Effect of L-Arginine on Titin Expression in Rat Soleus Muscle After Hindlimb Unloading

Nanosurgical Manipulation of Titin and Its M-Complex

High-Speed Atomic Force Microscopy to Study Myosin Motility

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