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Multiple C2 domains transmembrane protein 1 is expressed in CNS neurons and possibly regulates cellular vesicle retrieval and oxidative stress.

Authors: Qiu, Lifeng  Yu, Hanry  Liang, Fengyi 
Citation: Qiu L, etal., J Neurochem. 2015 Nov;135(3):492-507. doi: 10.1111/jnc.13251. Epub 2015 Sep 3.
Pubmed: (View Article at PubMed) PMID:26195140
DOI: Full-text: DOI:10.1111/jnc.13251

Multiple C2 domains transmembrane protein 1 (MCTP1) contains two transmembrane regions and three C2 domains of high Ca(2+)-binding affinity. Single-nucleotide polymorphism (SNP) of human MCTP1 gene is reportedly associated with bipolar disorder, but expression and function of MCTP1 in the CNS is still largely unknown. We cloned rat MCTP1 isoforms, and studied expression of MCTP1 transcript and protein in the CNS. Subcellular distribution and functional roles of MCTP1 were investigated in cultured primary neurons or PC12 cells by over-expression, cell imaging, and flow cytometry. MCTP1 immunostaining was seen in both CNS neuronal cell bodies and processes, especially in the hippocampus, dentate gyrus, medial habenular nucleus, amygdala, and selected cerebral and cerebellar cortical areas/layers. Under an electron microscope, MCTP1 immunoreactivity was observed on vesicles in neuronal cell bodies and pre-synaptic axon terminals. In cultured primary neurons and PC12 cells MCTP1 was detected on selected populations of secretory vesicles and endosomes. MCTP1 over-expression significantly inhibited neuronal transferrin endocytosis, secretory vesicle retrieval, cell migration, and oxidative stress from glutamate toxicity. Thus MCTP1 might be involved in regulating endocytic recycling of specific CNS neurons and synapses. MCTP1 abnormality might cause altered synaptic vesicle recycling, and thereby lead to vulnerability to neuropsychiatric diseases.


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RGD Object Information
RGD ID: 13210552
Created: 2017-09-02
Species: All species
Last Modified: 2017-09-02
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.