Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture

Mochida, Sumiko; Kobayashi, Haruo; Matsuda, Yuzuru; Yuda, Yasukatsu; Muramoto, Koji; Nonomura, Yoshiaki

doi:10.1016/0896-6273(94)90051-5

Cited by 145 publications

(141 citation statements)

References 52 publications

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“…The soma is occasionally surrounded by dynamin 1-expressing neurites (Fig. 1E, lower panels) of adjacent neurons (21)(22)(23). Similar to dynamin 1, dynamin 2 and 3 are detected by their specific antibody equivalently in SCG neurons in both the soma (Fig.…”

Section: Resultsmentioning

confidence: 90%

Dynamin Isoforms Decode Action Potential Firing for Synaptic Vesicle Recycling

Tanifuji

Funakoshi‐Tago

Ueda

et al. 2013

Journal of Biological Chemistry

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Background: The molecular mechanism linking variation in presynaptic neuronal activity to vesicle trafficking is unknown. Results: Three isoforms of dynamin, an essential endocytic protein, mediate vesicle reuse, having distinct rate and time constants with physiological action potential frequencies. Conclusion: Dynamin isoforms select appropriate vesicle reuse pathways associated with specific neuronal firing patterns. Significance: Individual dynamin isoforms regulate distinct synaptic vesicle reuse pathways that cover the full range of physiological action potential frequencies.

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Section: Resultsmentioning

confidence: 90%

Dynamin Isoforms Decode Action Potential Firing for Synaptic Vesicle Recycling

Tanifuji

Funakoshi‐Tago

Ueda

et al. 2013

Journal of Biological Chemistry

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“…Early reports, for example, identified myosin 2 in isolated synaptic junctions (Beach et al 1981), suggesting the possibility of presynaptic or postsynaptic roles, or both. Functional blockade of cholinergic synapses in cultured rat superior cervical ganglion neurons suggested a role for myosin 2 in presynaptic neurotransmitter release (Mochida et al 1994). The morphology of synaptic architecture in these same neurons, but as seen in myosin 5a null mice, appeared normal (Takagishi et al 2005).…”

Section: Synaptic Transmission Vesicle Trafficking and Viral Egressmentioning

confidence: 91%

Conventional myosins – unconventional functions

et al. 2010

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While the discovery of unconventional myosins raised expectations that their actions were responsible for most aspects of actin-based cell motility, few anticipated the wide range of cellular functions that would remain the purview of conventional two-headed myosins. The three nonsarcomeric, cellular myosins-M2A, M2B and M2C-participate in diverse roles including, but not limited to: neuronal dynamics, axon guidance and synaptic transmission; endothelial cell migration; cell adhesion, polarity, fusion and cytokinesis; vesicle trafficking and viral egress. These three conventional myosins each take on specific, differing functional roles during development and maturity, characteristic of each cell lineage; exact roles depend on the developmental stage of the cell, cellular location, upstream regulatory controls, relative isoform expression, orientation and associated state of the actin cytoscaffolds in which these myosins operate. Here, we discuss the separate yet related roles that characterise the actions of M2A, M2B and M2C in various cell types and show that these conventional myosins are responsible for functions as unconventional as any performed by unconventional myosins.

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“…Myosin II has also been reported to exist in growth cones of rat DRG neurons (Miller et al, 1992) and in presynaptic axon terminals of sympathetic ganglion cells (Mochida et al, 1994). Actin has also been identi®ed near synaptic vesicles (Burns & Augustine, 1995).…”

Section: Discussionmentioning

confidence: 99%

“…Phosphorylation of myosin II may also be involved in neurotransmitter release from presynaptic nerve terminals, since wortmannin inhibited synaptic transmission in the superior cervical ganglion of the rat (Mochida et al, 1994). However, whether myosin phosphorylation is involved in synaptic transmission in the central nervous system is not known.…”

Section: Introductionmentioning

confidence: 99%

“…The anti-SP antibody was also reported to react speci®cally with SP in the rat spinal cord (Cuello et al, 1979), but not with other peptides such as Leuor Met-enkephalin (see manufacturer's product description). Characterization of the anti-myosin II rabbit antibody was described elsewhere (Kumakura et al, 1994;Mochida et al, 1994). Immunoblotting of homogenates from various kinds of tissues including nervous system showed that the antibody binds to a single band of 200 KDa, which corresponds to the molecular weight of mysoin II heavy chain.…”

Section: Immuno¯uorescent Experimentsmentioning

confidence: 99%

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Differential effects of wortmannin on the release of substance P and amino acids from the isolated spinal cord of the neonatal rat

Suzuki

Yoshioka

Maehara

et al. 1998

British J Pharmacology

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1 E ects of wortmannin, an inhibitor of myosin light chain kinase, on the release of substance P and amino acids, GABA and glutamate, were investigated in the isolated spinal cord preparation of the neonatal rat. 2 Wortmannin at 0.5 ± 10 mM depressed the release of substance P evoked by high-K + (90 mM) medium from the spinal cord (IC 50 =1.1 mM). Wortmannin also depressed the high-K + (70 mM)-evoked release of substance P from cultured dorsal root ganglion neurons of neonatal rats. In contrast, the high-K + (90 mM)-evoked release of GABA and glutamate from the spinal cord was not a ected by wortmannin (0.1 ± 10 mM). 3 Upon stimulation of a dorsal root, a monosynaptic re¯ex and a subsequent slow ventral root depolarization were evoked in the ipsilateral ventral root of the same segment in the isolated spinal cord preparation. The magnitude of the slow ventral root depolarization was depressed gradually to about 70% of the control during the course of 30 min under wortmannin (1 mM). In contrast, the monosynaptic re¯ex was una ected by wortmannin. 4 Immuno¯uorescent staining revealed that immunoreactivities of substance P and myosin II were colocalized at presynaptic terminals in the dorsal horn of the neonatal rat spinal cord. 5 The present results suggest that myosin phosphorylation by myosin light chain kinase may play a crucial role in the release of substance P, but not in the release of GABA and glutamate in the neonatal rat spinal cord. This may re¯ect a di erence in the exocytic mechanisms of substance Pcontaining large dense core vesicles and amino acid-containing small clear vesicles.

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Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture

Cited by 145 publications

References 52 publications

Dynamin Isoforms Decode Action Potential Firing for Synaptic Vesicle Recycling

Dynamin Isoforms Decode Action Potential Firing for Synaptic Vesicle Recycling

Conventional myosins – unconventional functions

Differential effects of wortmannin on the release of substance P and amino acids from the isolated spinal cord of the neonatal rat

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