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-Structure paper
タイトル | Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse. |
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ジャーナル・号・ページ | Cell, Vol. 173, Issue 3, Page 735-748.e15, Year 2018 |
掲載日 | 2018年4月19日 |
![]() | Jingxian Li / Moran Shalev-Benami / Richard Sando / Xian Jiang / Amanuel Kibrom / Jie Wang / Katherine Leon / Christopher Katanski / Olha Nazarko / Yue C Lu / Thomas C Südhof / Georgios Skiniotis / Demet Araç / ![]() |
PubMed 要旨 | Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-Å cryoelectron microscopy structure of the human TEN2 ...Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-Å cryoelectron microscopy structure of the human TEN2 extracellular region (ECR), revealing a striking similarity to bacterial Tc-toxins. The ECR includes a large β barrel that partially encapsulates a C-terminal domain, which emerges to the solvent through an opening in the mid-barrel region. An immunoglobulin (Ig)-like domain seals the bottom of the barrel while a β propeller is attached in a perpendicular orientation. We further show that an alternatively spliced region within the β propeller acts as a switch to regulate trans-cellular adhesion of TEN2 to latrophilin (LPHN), a transmembrane receptor known to mediate critical functions in the central nervous system. One splice variant activates trans-cellular signaling in a LPHN-dependent manner, whereas the other induces inhibitory postsynaptic differentiation. These results highlight the unusual structural organization of TENs giving rise to their multifarious functions. |
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手法 | EM (単粒子) |
解像度 | 3.1 Å |
構造データ | |
化合物 | ![]() ChemComp-NAG: ![]() ChemComp-MAN: |
由来 |
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![]() | MEMBRANE PROTEIN / Teneurin / CNS |