Cbln1 is essential for synaptic integrity and plasticity in the cerebellum

Hirokazu Hirai, Zhen Pang, Dashi Bao, Taisuke Miyazaki, Leyi Li, Eriko Miura, Jennifer Parris, Yongqi Rong, Masahiko Watanabe, Michisuke Yuzaki, James I. Morgan

Research output: Contribution to journalArticlepeer-review

255 Citations (Scopus)


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, GluRδ2, 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.

Original languageEnglish
Pages (from-to)1534-1541
Number of pages8
JournalNature Neuroscience
Issue number11
Publication statusPublished - 2005 Nov

ASJC Scopus subject areas

  • Neuroscience(all)


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