ArticleThe Journal of cell biology1994
A signal located within amino acids 1-27 of GAD65 is required for its targeting to the Golgi complex region.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 61 citations in OpenAlex.
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- Tonic Dopamine Sensing Reveals a D2/D3 Mediated Dopamine Response to Raclopride in ClockΔ19 Mice Model.Research square · 2025Article
- Two distinct mechanisms target GAD67 to vesicular pathways and presynaptic clusters.The Journal of cell biology · 2010Article
- Role of the proteasome in excitotoxicity-induced cleavage of glutamic acid decarboxylase in cultured hippocampal neurons.PloS one · 2010Article
- Glutamate decarboxylase: loss of N-terminal segment does not affect homodimerization and determination of the oxidation state of cysteine residues.Neurochemical research · 2005Article
- Article
- Normal incidence of diabetes in NOD mice tolerant to glutamic acid decarboxylase.The Journal of experimental medicine · 2003Article
- A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65.The Journal of cell biology · 2002Article
- A proline-rich region and nearby cysteine residues target XLalphas to the Golgi complex region.Molecular biology of the cell · 2000Article
- Localization of a peripheral membrane protein: Gbetagamma targets Galpha(Z).Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Molecular characterization of caveolin association with the Golgi complex: identification of a cis-Golgi targeting domain in the caveolin molecule.The Journal of cell biology · 1999Article
- Trafficking of an acylated cytosolic protein: newly synthesized p56(lck) travels to the plasma membrane via the exocytic pathway.The Journal of cell biology · 1999Article
- The Caenorhabditis elegans gene unc-25 encodes glutamic acid decarboxylase and is required for synaptic transmission but not synaptic development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- Targeting of a short peptide derived from the cytoplasmic tail of the G1 membrane glycoprotein of Uukuniemi virus (Bunyaviridae) to the Golgi complex.Journal of virology · 1998Article
- Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase.Protein science : a publication of the Protein Society · 1998Article
- Localization of proteins to the Golgi apparatus.Trends in cell biology · 1998Review
- The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: a green fluorescent protein study.The Journal of cell biology · 1997Article
- Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4.The Journal of cell biology · 1997Article
- Activity-independent segregation of excitatory and inhibitory synaptic terminals in cultured hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1996Article
- GAD, diabetes, and Stiff-Man syndrome: some progress and more questions.Journal of endocrinological investigationReview
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 autoantigen in two autoimmune diseases: Stiff-Man syndrome and insulin-dependent diabetes mellitus. GAD65 is expressed in neurons and in pancreatic beta-cells, where it is concentrated in the Golgi complex region and in proximity to GABA-containing vesicles. GAD65, but not the similar isoform GAD67 which has a more diffuse cytosolic distribution, is palmitoylated within its first 100 amino acids (a.a.). We have previously demonstrated that the domain corresponding to a.a. 1-83 of GAD65 is required for the targeting of GAD65 to the Golgi complex region. Here we show that this domain is sufficient to target an unrelated protein, beta-galactosidase, to the same region. Site-directed mutagenesis of all the putative acceptor sites for thiopalmitoylation within this domain did not abolish targeting of GAD65 to the Golgi complex region. The replacement of a.a. 1-29 of GAD67 with the corresponding a.a. 1-27 of GAD65 was sufficient to target the otherwise soluble GAD67 to the Golgi complex region. Conversely, the replacement of a.a. 1-27 of GAD65 with a.a. 1-29 of GAD67 resulted in a GAD65 protein that had a diffuse cytosolic distribution and was primarily hydrophilic, suggesting that targeting to the Golgi complex region is required for palmitoylation of GAD65. We propose that the domain corresponding to a.a. 1-27 of GAD65, contains a signal required for the targeting of GAD65 to the Golgi complex region.
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