Structure of Slitrk2-PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion

Sci Rep. 2015 May 19:5:9686. doi: 10.1038/srep09686.

Abstract

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) δ. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Humans
  • Mice
  • Models, Molecular*
  • Protein Binding
  • Protein Conformation*
  • Protein Interaction Domains and Motifs
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2 / chemistry*
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2 / genetics
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2 / metabolism
  • Repressor Proteins / chemistry
  • Repressor Proteins / metabolism
  • Structure-Activity Relationship
  • Synapses / physiology*

Substances

  • LRR1 protein, human
  • Repressor Proteins
  • Ptprd protein, mouse
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2

Associated data

  • PDB/4Y61