| First Author | Hirai H | Year | 2005 |
| Journal | Nat Neurosci | Volume | 8 |
| Issue | 11 | Pages | 1534-41 |
| PubMed ID | 16234806 | Mgi Jnum | J:102516 |
| Mgi Id | MGI:3607685 | Doi | 10.1038/nn1576 |
| Citation | Hirai H, et al. (2005) Cbln1 is essential for synaptic integrity and plasticity in the cerebellum. Nat Neurosci 8(11):1534-41 |
| abstractText | 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 delta2, 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. |
