A family of ras-like GTP-binding proteins expressed in electromotor neurons
Open accessAbstract
The cDNAs encoding seven low molecular weight (LMW) GTP-binding proteins were isolated from an electrode lobe library of the marine ray Discopyge ommata. Four were assigned as the ray homologues of previously identified LMW GTP-binding proteins rab1, ral, Krev, and rho. Three others showed unique sequences, including two exhibiting significant similarity to the yeast SEC4 protein. Northern analysis indicated that several of the transcripts are enriched in neural tissues with a moderate level of expression in cardiac muscle. This tissue distribution was corroborated with affinity purified antibodies against the LMW GTP-binding proteins. Subcellular fractionation revealed that the proteins co-purify with cholinergic synaptic vesicles. Immunohistochemical analysis confirms this localization. At least two of the proteins, oral and o-rho, are localized to the pre-synaptic terminals.
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Ral is expressed in the nervous system.
“Like the exocyst, Ral is expressed in the nervous system (Ngsee et al, 1991;Huber et al, 1994;Peng et al, 2004;Han et al, 2009).”
From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Ngsee et al, 1991
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Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211 · see citing works
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Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst
Teodoro, R. O., Pekkurnaz, G., Nasser, A., Higashi‐Kovtun, M. E., Balakireva, M., McLachlan, I. G., Camonis, J., & Schwarz, T. L. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.147 · Cited by 61 · see citing works
Ral signaling pathway in health and cancer
Moghadam, A. R., Patrad, E., Tafsiri, E., Peng, W., Fangman, B., Pluard, T. J., Accurso, A., Salacz, M., Shah, K., Ricke, B., et al. (2017) · Cancer Medicine · doi:10.1002/cam4.1105 · Cited by 58 · see citing works
- Authors
- Ngsee, J. K., Elferink, L. A., & Scheller, R. H.
- Affiliations
- Stanford University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-02
- Volume
- 266
- Issue
- 4
- Pages
- 2675-2680
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1608131302
- Cited by
- 69
- References
- 1
- Citations by year
- 2019: 2 · 2017: 1 · 2015: 2 · 2013: 2
- FWCI
- 3.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- small GTPases, Rab1, Ral, Rho, cholinergic synaptic vesicles, presynaptic terminals, tissue distribution, myocardium, cDNA cloning
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Fractionation, Chromatography, Gel, Cross Reactions, Immunohistochemistry, Molecular Sequence Data, Neurons, Genes, ras, Sequence Homology, Nucleic Acid, Synaptic Vesicles, Torpedo, Transcription, Genetic, Blotting, Northern, Blotting, Western, Gene Expression, Polymerase Chain Reaction, GTP-Binding Proteins
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