期刊
NATURE NEUROSCIENCE
卷 8, 期 11, 页码 1534-1541出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nn1576
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资金
- NCI NIH HHS [CA 21765] Funding Source: Medline
- NIEHS NIH HHS [ES10772] Funding Source: Medline
- NINDS NIH HHS [NS040361, NS040749, NS042828] Funding Source: Medline
Cbln1 is a cerebellum-specific protein of previously unknown function that is structurally related to the C1q and tumor necrosis factor families of proteins. We show that Cbln1 is a glycoprotein secreted from cerebellar granule cells that is essential for three processes in cerebellar Purkinje cells: the matching and maintenance of pre- and postsynaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Notably, the phenotype of cbln1-null mice mimics loss-of-function mutations in the orphan glutamate receptor, GluR delta 2, a gene selectively expressed in Purkinje neurons. Therefore, Cbln1 secreted from presynaptic granule cells may be a component of a transneuronal signaling pathway that controls synaptic structure and plasticity.
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