Structural highlights
Function
[SLIK2_MOUSE] Suppresses neurite outgrowth.[1]
Publication Abstract from PubMed
Selective binding between pre- and postsynaptic adhesion molecules can induce synaptic differentiation. Here we report the crystal structure of a synaptogenic trans-synaptic adhesion complex between Slit and Trk-like family member 2 (Slitrk2) and receptor protein tyrosine phosphatase (RPTP) delta. The structure and site-directed mutational analysis revealed the structural basis of splicing-dependent adhesion between Slitrks and type IIa RPTPs for inducing synaptic differentiation.
Structure of Slitrk2-PTPdelta complex reveals mechanisms for splicing-dependent trans-synaptic adhesion.,Yamagata A, Sato Y, Goto-Ito S, Uemura T, Maeda A, Shiroshima T, Yoshida T, Fukai S Sci Rep. 2015 May 19;5:9686. doi: 10.1038/srep09686. PMID:25989451[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Aruga J, Mikoshiba K. Identification and characterization of Slitrk, a novel neuronal transmembrane protein family controlling neurite outgrowth. Mol Cell Neurosci. 2003 Sep;24(1):117-29. PMID:14550773
- ↑ Yamagata A, Sato Y, Goto-Ito S, Uemura T, Maeda A, Shiroshima T, Yoshida T, Fukai S. Structure of Slitrk2-PTPdelta complex reveals mechanisms for splicing-dependent trans-synaptic adhesion. Sci Rep. 2015 May 19;5:9686. doi: 10.1038/srep09686. PMID:25989451 doi:http://dx.doi.org/10.1038/srep09686
