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001-es BibID:	BIBFORM121062
035-os BibID:	(Scopus)85192031398 (WoS)001258453900001
Első szerző:	De Gasperi, Rita
Cím:	Septin 7 interacts with Numb to preserve sarcomere structural organization and muscle contractile function / Rita De Gasperi, Laszlo Csernoch, Beatrix Dienes, Monika Gonczi, Jayanta K. Chakrabarty, Shahar Goeta, Abdurrahman Aslan, Carlos A. Toro, David Karasik, Lewis M. Brown, Marco Brotto, Christopher P. Cardozo
Dátum:	2024
ISSN:	2050-084X
Megjegyzések:	Here, we investigated the mechanisms by which aging-related reductions of the levels of Numb in skeletal muscle fibers contribute to loss of muscle strength and power, two critical features of sarcopenia. Numb is an adaptor protein best known for its critical roles in development, including asymmetric cell division, cell-type specification, and termination of intracellular signaling. Numb expression is reduced in old humans and mice. We previously showed that, in mouse skeletal muscle fibers, Numb is localized to sarcomeres where it is concentrated near triads; conditional inactivation of Numb and a closely related protein Numb-like (Numbl) in mouse myofibers caused weakness, disorganization of sarcomeres, and smaller mitochondria with impaired function. Here, we found that a single knockout of Numb in myofibers causes reduction in tetanic force comparable to a double Numb, Numbl knockout. We found by proteomics analysis of protein complexes isolated from C2C12 myotubes by immunoprecipitation using antibodies against Numb that Septin 7 is a potential Numb-binding partner. Septin 7 is a member of the family of GTP-binding proteins that organize into filaments, sheets, and rings, and is considered part of the cytoskeleton. Immunofluorescence evaluation revealed a partial overlap of staining for Numb and Septin 7 in myofibers. Conditional, inducible knockouts of Numb led to disorganization of Septin 7 staining in myofibers. These findings indicate that Septin 7 is a Numb-binding partner and suggest that interactions between Numb and Septin 7 are critical for structural organization of the sarcomere and muscle contractile function.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk animals metabolism mice genetics Intracellular Signaling Peptides and Proteins signal peptide Membrane Proteins physiology skeletal muscle Protein Binding Muscle Contraction skeletal CYTOSKELETON knockout mouse Nerve Tissue Proteins nerve protein knockout CELL BIOLOGY Muscle Fibers sarcomere Septins skeletal muscle cell Excitation-contraction coupling numb septin sarcomere structure NUMB protein sept7 protein
Megjelenés:	eLife. - 12 (2024), p. RP89424. -
További szerzők:	Csernoch László (1961-) (élettanász) Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Gönczi Mónika (1974-) (élettanász) Chakrabarty, Jayanta K. Goeta, Shahar Aslan, Abdurrahman Toro, Carlos A. Karasik, David Brown, Lewis M. Brotto, Marco Cardozo, Christopher P.
Pályázati támogatás:	2020-4.1.1-TKP2020 Egyéb K_137600 OTKA
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM103051
035-os BibID:	(Wos)000837832700001 (Scopus)85135422946
Első szerző:	Gönczi Mónika (élettanász)
Cím:	Septin7 is indispensable for proper skeletal muscle architecture and function / Mónika Gönczi, Zsolt Ráduly, László Szabó, János Fodor, Andrea Telek, Nóra Dobrosi, Norbert Balogh, Péter Szentesi, Gréta Kis, Miklós Antal, György Trencsenyi, Beatrix Dienes, László Csernoch
Dátum:	2022
ISSN:	2050-084X
Megjegyzések:	Today septins are considered as the fourth component of the cytoskeleton, with the Septin7 isoform playing a critical role in the formation of higher-order structures. While its importance has already been confirmed in several intracellular processes of different organs, very little is known about its role in skeletal muscle. Here, using Septin7 conditional knockdown (KD) mouse model, the C2C12 cell line, and enzymatically isolated adult muscle fibers, the organization and localization of septin filaments are revealed, and an ontogenesis-dependent expression of Septin7 is demonstrated. KD mice displayed a characteristic hunchback phenotype with skeletal deformities, reduction in in vivo and in vitro force generation, and disorganized mitochondrial networks. Furthermore, knockout of Septin7 in C2C12 cells resulted in complete loss of cell division while KD cells provided evidence that Septin7 is essential for proper myotube differentiation. These and the transient increase in Septin7 expression following muscle injury suggest that it may be involved in muscle regeneration and development.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk cell biology cytoskeleton development human mitochondria mouse regeneration septins skeletal muscle
Megjelenés:	eLife. - 11 (2022), p. e75863. -
További szerzők:	Ráduly Zsolt (1992-) (gyógyszerész) Szabó László (1994-) (molekuláris biológus) Fodor János (1973-) (élettanász, biotechnológus) Telek Andrea (1977-) (élettanász) Dobrosi Nóra (1981-) (molekuláris biológus) Balogh Norbert (1988-) (molekuláris biológus) Szentesi Péter (1967-) (élettanász) Kis Gréta (1979-) (molekuláris biológus) Antal Miklós (1951-) (orvos, anatómus) Trencsényi György (1978-) (biológus, biokémikus, molekuláris biológus) Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Csernoch László (1961-) (élettanász)
Pályázati támogatás:	TKP2020-NKA-04 Egyéb 2020-4.1.1-TKP2020 Egyéb K-137600 OTKA GINOP-2.3.2-15-2016-00044 GINOP GINOP-2.3.3-15-2016-00020 GINOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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