The Presence of Septin Proteins in the Neuromuscular Junction of Somatic Muscle in the Earthworm Lumbricus terrestris
- Авторлар: Nurullin L.F1,2, Volkov E.M2
-
Мекемелер:
- Kazan Institute of Biochemistry and Biophysics, Kazan Scientific Center of the Russian Academy of Sciences
- Kazan State Medical University
- Шығарылым: Том 69, № 5 (2024)
- Беттер: 1011-1017
- Бөлім: Cell biophysics
- URL: https://archivog.com/0006-3029/article/view/676128
- DOI: https://doi.org/10.31857/S0006302924050088
- EDN: https://elibrary.ru/MKFQWM
- ID: 676128
Дәйексөз келтіру
Аннотация
Using fluorescent confocal microscopy it has been shown that proteins belonging to the septin family such as Septin 2, 3, 5, 7, and 9 are present in the somatic muscle of the earthworm Lumbricus terrestris. Septins 2 and 9 are associated with the lack of their specific concentrations in a cholinergic synapse, while septins 3, 5, and especially 7 levels correlate with quantitatively expressed binding in their localization to the motor end plate. It is assumed that Septins 3, 5 and, mostly, 7 can be involved in the mechanisms of modulation of quantal release of neurotransmitters.
Негізгі сөздер
Авторлар туралы
L. Nurullin
Kazan Institute of Biochemistry and Biophysics, Kazan Scientific Center of the Russian Academy of Sciences; Kazan State Medical University
Email: leniz2001@mail.ru
Kazan, 420111 Russia; Kazan, 420012 Russia
E. Volkov
Kazan State Medical University
Email: euroworm@mail.ru
Kazan, 420012 Russia
Әдебиет тізімі
- Grupp B. and Gronemeyer T. A biochemical view on the septins, a less known component of the cytoskeleton. Biol. Chem., 404 (1), 1–13 (2022). doi: 10.1515/hsz-2022-0263
- Cavini I. A., Leonardo D. A., Rosa H. V. D., Castro D. K. S. V., D'Muniz Pereira H., Valadares N. F., Araujo A. P. U., and Garratt R. C. The structural biology of septins and their filaments: an update. Front. Cell Dev. Biol., 9, 765085 (2021). doi: 10.3389/fcell.2021.765085
- Kartmann B. and Roth D. Novel roles for mammalian septins: from vesicle trafficking to oncogenesis. J. Cell. Sci., 114 (Pt 5), 839–844 (2001). doi: 10.1242/jcs.114.5.839
- Deb B. K. and Hasan G. Regulation of store-operated Ca2+ entry by septins. Front. Cell Dev. Biol., 4, 142 (2016). doi: 10.3389/fcell.2016.00142
- Deb B. K. and Hasan G. SEPT7-mediated regulation of Ca2+ entry through Orai channels requires other septin subunits. Cytoskeleton (Hoboken), 76 (1), 104– 114 (2019). doi: 10.1002/cm.21476
- Deb B. K., Chakraborty P., Gopurappilly R., and Hasan G. SEPT7 regulates Ca2+ entry through Orai channels in human neural progenitor cells and neurons. Cell Calcium, 90, 102252 (2020). doi: 10.1016/j.ceca.2020.102252
- Werner B. and Yadav S. Phosphoregulation of the septin cytoskeleton in neuronal development and disease. Cytoskeleton (Hoboken), 80 (7–8), 275–289 (2023). doi: 10.1002/cm.21728
- Nurullin L. F., Khuzakhmetova V. F., Khaziev E. F., Samigullin D. V., Tsentsevitsky A. N., Skorinkin A. I., Bukharaeva E. A., and Vagin O. Reorganization of septins modulates synaptic transmission at neuromuscular junctions. Neuroscience, 404, 91–101 (2019). doi: 10.1016/j.neuroscience.2019.01.060
- Volkov E. M. and Nurullin L. F. Effects of cholinergic receptor agonists and antagonists on miniature stimulatory postsynaptic ionic currents in somatic muscle cells of lumbricus terrestris. Bull. Exp. Biol. Med., 139 (3), 360–362 (2005). doi: 10.1007/s10517-005-0294-2
- Bennett M. R., Farnell L., and Gibson W. G. The probability of quantal secretion near a single calcium channel of an active zone. Biophys. J., 78 (5), 2201–2221 (2000). doi: 10.1016/S0006-3495(00)76769-5
- Parry L., Tanner A., and Vinther J. The origin of annelids. Front. Palaeontol., 57 (6), 1091–1103 (2014). doi: 10.1111/pala.12129
- Purschke G. and Müller M. C. Evolution of body wall musculature. Integr. Comp. Biol., 46 (4), 497–507 (2006). doi: 10.1093/icb/icj053
- Nurullin L. F., Almazov N. D., and Volkov E.M. Immunofluorescent identification of GABAergic structures in the somatic muscle of the earthworm Lumbricus terrestris. Biochemistry (Moscow). Suppl. Ser. A Membr. Cell. Biol., 17 (3), 208–213 (2023). doi: 10.1134/S1990747823040074, EDN: GMIYPL
- Volkov E. M., Nurullin L. F., Svandová I., and Vyskocil F. Participation of electrogenic Na+-K+ATPase in the membrane potential of earthworm body wall muscles. Physiol. Res., 49 (4), 481–484 (2000). EDN: LGGZWJ
- Grigoryev P. N., Khisamieva G. A., and Zefirov A.L. Septin polymerization slows synaptic vesicle recycling in motor nerve endings. Acta Naturae., 11 (2), 54–62 (2019). doi: 10.32607/20758251-2019-11-2-54-62, EDN: UWFOQK
- Beites C. L., Campbell K. A., and Trimble W. S. The septin Sept5/CDCrel-1 competes with alpha-SNAP for binding to the SNARE complex. Biochem. J., 385 (Pt 2), 347–353 (2005). doi: 10.1042/BJ20041090
- Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I., Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., and Nagata K. Sept8 controls the binding of vesicle-associated membrane protein 2 to synaptophysin. J. Neurochem., 108 (4), 867–880 (2009). doi: 10.1111/j.1471-4159.2008.05849.x
- Maimaitiyiming M., Kobayashi Y., Kumanogoh H., Nakamura S., Morita M., and Maekawa S. Identification of dynamin as a septin-binding protein. Neurosci. Lett., 534, 322–326 (2013). doi: 10.1016/j.neulet.2012.12.002
Қосымша файлдар
