Interaction of NAP-22 with brain glutamic acid decarboxylase (GAD)

被引：12

作者：

Maekawa, Shohei ^{[1
]}

Kobayashi, Yuumi ^{[1
]}

Odagaki, Sin-Ichi ^{[1
]}

Makino, Midori ^{[1
]}

Kumanogoh, Haruko ^{[2
]}

Nakamura, Shun ^{[3
]}

Morita, Mitsuhiro ^{[1
]}

Hayashi, Fumio ^{[1
]}

机构：

[1] Kobe Univ, Grad Sch Sci, Dept Biol, Kobe, Hyogo 6578501, Japan

[2] Natl Ctr Neurol & Psychiat, Natl Inst Neurosci, Div Biochem & Cellular Biol, Kodaira, Tokyo 1870031, Japan

[3] Tokyo Univ Agr & Technol, Dept Biotechnol & Life Sci, Koganei, Tokyo, Japan

来源：

NEUROSCIENCE LETTERS | 2013年 / 537卷

关键词：

Lipid raft; GAD65/67; NAP-22; Synapse; CALMODULIN-BINDING PROTEIN; GAMMA-AMINOBUTYRIC-ACID; CLEFT-PALATE; MICE LACKING; ISOFORM; BASP1; PHOSPHORYLATION; LOCALIZATION; PURIFICATION; MARCKS;

D O I：

10.1016/j.neulet.2013.01.030

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

NAP-22 (also called BASP1 or CAP-23) is a neuron-enriched protein localized mainly in the synaptic vesicles and the synaptic plasma membrane. Biochemically, it is recovered in the lipid raft fraction. In order to understand the physiological function of the neuronal lipid raft, NAP-22 binding proteins were screened with a pull-down assay. Glutamic acid decarboxylase (GAD) was detected through LC-MS/MS, and Western blotting using a specific antibody confirmed the result. Two isoforms of GAD, GAD65 and GAD67, were expressed in bacteria as GST-fusion forms and the interaction with NAP-22 was confirmed in vitro. Partial co-localization of NAP-22 with GAD65 and GAD67 was also observed in cultured neurons. The binding showed no effect on the enzymatic activity of GAD65 and GAD67. These results hence suggest that NAP-22 could participate in the transport of GAD65 and GAD67 to the presynaptic termini and their retention on the synaptic vesicles as an anchoring protein. (c) 2013 Elsevier Ireland Ltd. All rights reserved.

引用

页码：50 / 54

页数：5

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