Receptor-type tyrosine-protein phosphatases

Stable Identifier
Homo sapiens
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Like neurexins, Receptor-like protein tyrosine phosphatases (RPTPs) make trans-synaptic adhesion complexes with multiple postsynaptic binding partners to regulate synapse organization. The type IIa RPTPs include three members, Receptor-type tyrosine-protein phosphatase F (PTPRF) sometimes referred to as leukocyte common antigen-related (LAR), Receptor-type tyrosine-protein phosphatase sigma (PTPRS) and Receptor-type tyrosine-protein phosphatase delta (PTPRD). These proteins contain typical cell adhesion immunoglobulin-like (Ig) and fibronectin III (FNIII) domains, suggesting the involvement of RPTPs in cell-cell and cell-matrix interactions. To date, six different types of postsynaptic organizers for type-IIa RPTPs have been reported: interleukin-1 receptor accessory protein (IL1RAP, IL-1RAcP) (Yoshida et al. 2012), IL-1RAcP-like-1 (IL1RAPL1) (Yoshida et al. 2011), Neurotrophin receptor tyrosine kinase 3 (NTRK3, TrkC) (Takahashi et al. 2011), Leucine-rich repeat-containing protein 4B (LRRC4B, Netrin-G ligand-3, NGL-3) (Woo et al. 2009, Kwon et al. 2010), the Slit- and Trk-like (Slitrk) family proteins (Takahashi et al. 2012, Yim et al. 2013, Yamagata et al. 2015) and the liprins (Serra-Pagès et al. 1998, Dunah et al. 2005).

Literature References
PubMed ID Title Journal Year
23835198 Protein tyrosine phosphatases PTPδ, PTPσ, and LAR: presynaptic hubs for synapse organization

Takahashi, H, Craig, AM

Trends Neurosci. 2013
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