Expression and localisation of dynamin and syntaxin during neural development and neuromuscular synapse formation

Noakes, Peter G.; Chin, David Y.; Kim, S.S.; Liang, Simon; Phillips, William D.

doi:10.1002/(sici)1096-9861(19990809)410:4<531::aid-cne2>3.0.co;2-c

Cited by 30 publications

(13 citation statements)

References 44 publications

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“…Dynamin 1 is almost exclusively expressed in neurons, dynamin 2 is found in the brain but is also widely expressed among other tissues and dynamin 3 was initially identified in testis but is also found in brain, lung, and heart. Because of its restriction to neurons, dynamin 1 has been assumed to be the synaptic isoform of dynamin expressed in neurons after maturation and in the adult brain [43][44][45]. Although the majority of studies implicate dynamin in endocytosis, there is evidence that dynamin may exert additional functions in cell physiology.…”

Section: Discussionmentioning

confidence: 99%

The rat brain hippocampus proteome

Fountoulakis

Tsangaris

Maris

et al. 2005

Journal of Chromatography B

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Section: Discussionmentioning

confidence: 99%

The rat brain hippocampus proteome

Fountoulakis

Tsangaris

Maris

et al. 2005

Journal of Chromatography B

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“…It is well established that syntaxin 1 functions as a synaptic t-SNARE to mediate synaptic vesicle exocytosis at nerve terminals (13)(14)(15). Syntaxin 1 appears early during embryonic development (16,17), and its expression level is dramatically up-regulated during synapse formation and brain maturation (16 -19). Regulation of syntaxin 1 levels may contribute to the mechanism underlying learning and memory, since changes in syntaxin 1 levels have been found to correlate with long term potentiation and various learning and memory behaviors (20 -22).…”

mentioning

confidence: 99%

Staring, a Novel E3 Ubiquitin-Protein Ligase That Targets Syntaxin 1 for Degradation

Chin

Vavalle

Lian

2002

Journal of Biological Chemistry

107

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Syntaxin 1 is an essential component of the neurotransmitter release machinery, and regulation of syntaxin 1 expression levels is thought to contribute to the mechanism underlying learning and memory. However, the molecular events that control the degradation of syntaxin 1 remain undefined. Here we report the identification and characterization of a novel RING finger protein, Staring, that interacts with syntaxin 1. Staring is expressed throughout the brain, where it exists in both cytosolic and membrane-associated pools. Staring binds and recruits the brain-enriched E2 ubiquitin-conjugating enzyme UbcH8 to syntaxin 1 and facilitates the ubiquitination and proteasome-dependent degradation of syntaxin 1. These findings suggest that Staring is a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation by the ubiquitin-proteasome pathway.Modulation of protein degradation is a major mechanism by which cells regulate the expression levels of specific proteins and consequently the cellular processes that these proteins participate in (1, 2). The ubiquitin-proteasome pathway plays a crucial role in the degradation of proteins involved in a variety of cellular processes, including differentiation, proliferation, and apoptosis. However, the role of the ubiquitin-proteasome pathway in the degradation of presynaptic proteins remains poorly characterized, despite the presence of ubiquitin at nerve terminals (3-5). In the ubiquitin-proteasome pathway, substrates are marked for degradation by covalent linkage to ubiquitin. The ubiquitinated substrate proteins are then recognized and degraded by the 26 S proteasome (1, 2, 6). Ubiquitination involves a highly specific enzyme cascade in which ubiquitin is first activated by an E1 1 ubiquitin-activating enzyme and then transferred to an E2 ubiquitin-conjugating enzyme and finally ligated to the substrate by an E3 ubiquitin-protein ligase (1,7,8). The E3 ubiquitin-protein ligase plays an essential role in determining the specificity of ubiquitination and subsequent protein degradation. Consistent with this role, it is estimated that an organism such as a human contains over 100 E3 ubiquitin ligases, in contrast to a single E1 ubiquitin-activating enzyme and about a dozen E2 ubiquitin-conjugating enzymes (9). Despite the importance of E3 ubiquitin-protein ligases in specific protein degradation and the estimated presence of more than 100 E3 ligases in the human genome, only a few E3 ligases have been characterized at the molecular level.Syntaxin 1 is a neuronal membrane protein that was originally identified as a binding partner for synaptotagmin and the N-type calcium channel (10 -12). It is well established that syntaxin 1 functions as a synaptic t-SNARE to mediate synaptic vesicle exocytosis at nerve terminals (13)(14)(15). Syntaxin 1 appears early during embryonic development (16, 17), and its expression level is dramatically up-regulated during synapse formation and brain maturation (16 -19). Regulation of syntaxin 1 levels may contribute to the mechanism unde...

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“…Interestingly, the upregulation of dynamin I during neuronal development is delayed when compared with the expression of other synaptic vesicle trafficking proteins (Bergmann et al 1999;Noakes et al 1999), indicating that dynamin is mainly required during late stages of synaptic maturation coincident with the beginning of highly regulated vesicle endocytosis. Hence, based on the dynamin-I-staining pattern in the developing pineal gland, our investigation has provided some clues concerning the probable onset of regulated exo-/endocytotic cycles of SLMVs.…”

Section: Discussionmentioning

confidence: 99%

Expression of synaptic vesicle trafficking proteins in the developing rat pineal gland

Redecker

2000

Cell and Tissue Research

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Adult mammalian pinealocytes contain several synaptic membrane proteins that are probably involved in the regulation of targeting and exocytosis of synaptic-like microvesicles (SLMVs). Immunohistochemical techniques have now demonstrated the spatiotemporal expression pattern of some of these proteins during rat pineal ontogenesis. Various synaptic vesicle trafficking proteins are detectable in proliferating epithelial cells of the pineal anlage even at embryonic day 17.5 (E 17.5), with the exception of syntaxin I (weakly expressed from E 19.5) and dynamin I (whose levels increase markedly during the first postnatal week). Numerous cells exhibiting strong immunoreactivity for synaptobrevin II, SNAP-25, synaptophysin, and munc-18-1 are distributed throughout the increasingly compact gland at E 19.5 and E 20.5; however, their number declines toward the proximal deep part of the organ. Groups of postmitotic cells situated at the surface of the developing gland exhibit marked immunoreactivity for the aforementioned proteins and lie close to the laminin-immunoreactive outer limiting basement membrane or to its remnants in regions of basement membrane dissolution. We also show that synthesis of vimentin and S-antigen seems to begin earlier during pineal development than previously recognized. Thus, synaptic vesicle trafficking proteins are the earliest molecular markers of pinealocyte differentiation known to date, being expressed well before the onset of rhythmic hormone secretion in the pineal gland, where they may play a role in morphogenetic events. Components of the extracellular matrix such as laminin may be critically involved in the upregulation of synaptic membrane protein expression. The dynamin immunostaining pattern indicates that SLMVs of pinealocytes begin to undergo regulated cycles of exo/endocytosis during postnatal week 1.

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Expression and localisation of dynamin and syntaxin during neural development and neuromuscular synapse formation

Cited by 30 publications

References 44 publications

The rat brain hippocampus proteome

The rat brain hippocampus proteome

Staring, a Novel E3 Ubiquitin-Protein Ligase That Targets Syntaxin 1 for Degradation

Expression of synaptic vesicle trafficking proteins in the developing rat pineal gland

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