All the three LAR-RPTP transmembrane tyrosine phosphatases associate with liprin proteins and colocalize with liprin-alpha1 at the proximal edges of focal adhesions. Based on sequence similarities and binding characteristics, liprins are subdivided into alpha-type and beta-type liprins. The C-terminal, non-coiled coil regions of alpha-liprins bind to the membrane-distal phosphatase domains of LAR family members, as well as to the C-terminal, non-coiled coil region of beta-liprins. Liprin is required for normal presynaptic differentiation in C. elegans and controls synapse morphogenesis in Drosophila. In mammalian synapses the functional significance of liprin and LAR-RPTP interaction is unknown (Pages et al. 1998, Dunah et al. 2005).
Debant, A, Serra-Pagès, C, Medley, Q, Kedersha, NL, Fazikas, L, Streuli, M
Wyszynski, M, Jaworski, J, Sheng, M, Hueske, E, Dunah, AW, Simonetta, A, Hoogenraad, CC, Liu, G, Pak, DT
Serra-Pagès, C, Hart, A, Medley, QG, Streuli, M, Tang, M
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