Unknown

Dataset Information

0

Structure of Slitrk2-PTP? complex reveals mechanisms for splicing-dependent trans-synaptic adhesion.


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) ?. 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.

SUBMITTER: Yamagata A 

PROVIDER: S-EPMC4437028 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Yamagata Atsushi A   Sato Yusuke Y   Goto-Ito Sakurako S   Uemura Takeshi T   Maeda Asami A   Shiroshima Tomoko T   Yoshida Tomoyuki T   Fukai Shuya S  

Scientific reports 20150519


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. ...[more]

Similar Datasets

| S-EPMC4423211 | biostudies-literature
| S-SCDT-EMBOJ-2019-104150 | biostudies-other
| S-EPMC3288805 | biostudies-literature
| S-EPMC4578660 | biostudies-literature
| S-EPMC5773591 | biostudies-literature
| S-EPMC7069723 | biostudies-literature
| S-EPMC3056349 | biostudies-literature
| S-EPMC3621762 | biostudies-literature
| S-EPMC4974644 | biostudies-literature
| S-EPMC5970233 | biostudies-literature