Targeting of the 67-kDa isoform of glutamic acid decarboxylase to intracellular organelles is mediated by its interaction with the NH2- terminal region of the 65-kDa isoform of glutamic acid decarboxylase

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Bibtex

@article{2a6eee77902c426b9c10b4a9537c373c,
title = "Targeting of the 67-kDa isoform of glutamic acid decarboxylase to intracellular organelles is mediated by its interaction with the NH2- terminal region of the 65-kDa isoform of glutamic acid decarboxylase",
abstract = "The two isoforms of glutamic acid decarboxylase (GAD), GAD67 and GAD65, synthesize the neurotransmitter γ-aminobutyric acid in neurons and pancreatic β-cells. Previous studies suggest that GAD67 is a soluble cytosolic protein, whereas GAD65 is membrane-associated. Here we study the intracellular distribution of GAD67 in neurons, pancreatic β-cells, and fibroblasts transfected either with GAD65 and GAD67 together or with GAD67 alone. Neuronal GAD67 is partially recovered with GAD65 in membrane- containing pellet fractions and Triton X-114 detergent phases. The two proteins coimmunoprecipitate from extracts of brain and GAD65-GAD67 cotransfected fibroblasts, but not when extracts of GAD65 and GAD67 transfected fibroblasts were mixed and used as a stating material for immunoprecipitation. GAD67 is concentrated in the Gorgi complex region in GAD65-GAD67 cotransfected fibroblasts, but not in fibroblasts transfected with GAD67 alone. A pool of neuronal GAD67 colocalizes with GAD65 in the Golgi complex region and in many synapses. The two proteins also colocalize in the perinuclear region of some pancreatic{\= }-cells. GAD67 interacts with the NH2-terminal region of GAD65, even in the absence of palmitoylation of this region of GAD65. Taken together, our results indicate that GAD65-GAD67 association occurs in vivo and is required for the targeting of GAD67 to membranes.",
author = "R. Dirkx and A. Thomas and L. Li and A. Lernmark and Sherwin, {R. S.} and {De Camilli}, P. and M. Solimena",
year = "1995",
month = jan,
day = "1",
doi = "10.1074/jbc.270.5.2241",
language = "English",
volume = "270",
pages = "2241--2246",
journal = "Journal of Biological Chemistry",
issn = "1083-351X",
publisher = "ASBMB",
number = "5",

}