LAR-RPTPs are not essential for synapse formation, but they are important determinants of synapse properties as they contribute to regulate postsynaptic NMDA receptor function.

The immunoglobulin superfamily cell surface protein Sticks and Stones is a binding partner for the Lar Drosophila receptor tyrosine phosphatase that mediates Lar's developmental functions at the larval neuromuscular junction, mushroom body, and adult optic lobe.

Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are precisely localized to synaptic appositions, but do not control the assembly and function of the presynaptic nerve terminal.

Two receptor tyrosine phosphatases having overlapping function for the determination of the final axon stabilizing layer is encoded for their cumulative cytoplasmic activity and ligand specificity in the visual system.

Systematic proteomic approaches identify several cell junction regulators as substrates for the homophilic receptor tyrosine phosphatase PTPRK and implicate its pseudophosphatase domain in substrate recognition.

Presynaptic adhesion molecule PTPσ in the hippocampus regulates postsynaptic NMDA receptor function and behavioral novelty recognition through mechanisms independent of their trans-synaptic binding partners.

R7 photoreceptors require the endosomal protein Lost and Found to form stable connections only when this protein is also present in neurons that are synaptic partners of R7.

A nerve bundle is not simply a cable of wires, but has order within it.

Mechanicals forces and local (Wnt) signaling can synergize to increase β-catenin signaling and produce unique growth phenotypes.