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Akademický článek
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Publikováno v:
The Journal of Neuroscience. 16:5905-5913
In nerve terminals, synaptic vesicles form large clusters anchored to the presynaptic plasmalemma. Recently, FM1-43 photobleaching experiments carried out at frog motor endplates demonstrated lack of lateral intermixing of synaptic vesicles within cl
Publikováno v:
Journal of Biological Chemistry. 271:6917-6924
At least three high affinity Na+- and Cl--dependent gamma-aminobutyric acid (GABA) transporters are known to exist in the rat and mouse brain. These transporters share 50-65% amino acid sequence identity with the kidney betaine transporter which also
Publikováno v:
Proceedings of the National Academy of Sciences. 93:331-335
Amphiphysin, a major autoantigen in paraneoplastic Stiff-Man syndrome, is an SH3 domain-containing neuronal protein, concentrated in nerve terminals. Here, we demonstrate a specific, SH3 domain-mediated, interaction between amphiphysin and dynamin by
Autor:
T J Chilcote, Lisa Edelmann, Peter S. McPherson, Kohji Takei, O Mundigl, P De Camilli, Thierry Galli
Publikováno v:
The Journal of Cell Biology
There is strong evidence to indicate that proteins of the synaptobrevin family play a key role in exocytosis. Synaptobrevin 1 and 2 are expressed at high concentration in brain where they are localized on synaptic vesicles. Cellubrevin, a very simila
Publikováno v:
The Journal of Cell Biology
The mechanisms involved in the targeting of proteins to different cytosolic compartments are still largely unknown. In this study we have investigated the targeting signal of the 65-kD isoform of glutamic acid decarboxylase (GAD65), a major autoantig
Publikováno v:
Journal of Cell Science. 1993:93-100
SUMMARY Neurons have at least two pathways of regulated secretion, which involve two classes of secretory organelles: typical synaptic vesicles (SVs) and large dense-core vesicles. Large dense-core vesicles store and secrete peptide neurotransmitters
Autor:
Pietro De Camilli, Gian Carlo Ochoa, O Mundigl, Vladimir I. Slepnev, Alexander V. Kabanov, Carol David
Publikováno v:
Scopus-Elsevier
Amphiphysin I is an SH3 domain-containing neuronal protein, enriched in axon terminals, which was reported to act as a physiological binding partner for dynamin I in synaptic vesicle endocytosis. Rvs167 and Rvs161, the yeast homologs of amphiphysin I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62395fd7a76c28a49c6ea37a6c07d6b6
https://europepmc.org/articles/PMC6793426/
https://europepmc.org/articles/PMC6793426/
Akademický článek
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Publikováno v:
The Journal of Cell Biology
Strong evidence implicates clathrin-coated vesicles and endosome-like vacuoles in the reformation of synaptic vesicles after exocytosis, and it is generally assumed that these vacuoles represent a traffic station downstream from clathrin-coated vesic