Structural highlights
Function
[CBLN4_MOUSE] May be involved in synaptic functions in the CNS. May play a role in CBLN3 export from the endoplasmic reticulum and secretion.
Publication Abstract from PubMed
Unlike cerebellin 1 (Cbln1), which bridges neurexin (Nrxn) receptors and delta-type glutamate receptors in a trans-synaptic triad, Cbln4 was reported to have no or weak binding for the receptors despite sharing approximately 70% sequence identity with Cbln1. Here, we report crystal structures of the homotrimers of the C1q domain of Cbln1 and Cbln4 at 2.2 and 2.3 A resolution, respectively. Comparison of the structures suggests that the difference between Cbln1 and Cbln4 in GluD2 binding might be because of their sequence and structural divergence in loop CD. Surprisingly, we show that Cbln4 binds to Nrxn1beta and forms a stable complex with the laminin, nectin, sex-hormone binding globulin (LNS) domain of Nrxn1beta. Furthermore, the negative-stain electron microscopy reconstruction of hexameric full-length Cbln1 at 13 A resolution and that of the Cbln4/Nrxn1beta complex at 19 A resolution suggest that Nrxn1beta binds to the N-terminal region of Cbln4, probably through strand beta10 of the S4 insert.
Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions.,Zhong C, Shen J, Zhang H, Li G, Shen S, Wang F, Hu K, Cao L, He Y, Ding J Cell Rep. 2017 Sep 5;20(10):2328-2340. doi: 10.1016/j.celrep.2017.08.031. PMID:28877468[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhong C, Shen J, Zhang H, Li G, Shen S, Wang F, Hu K, Cao L, He Y, Ding J. Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions. Cell Rep. 2017 Sep 5;20(10):2328-2340. doi: 10.1016/j.celrep.2017.08.031. PMID:28877468 doi:http://dx.doi.org/10.1016/j.celrep.2017.08.031
