PTPRF, PTPRS, PTPRD bind Liprins

Stable Identifier
R-HSA-388824
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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).
Literature References
PubMed ID Title Journal Year
7796809 The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions

Debant, A, Serra-Pagès, C, Medley, Q, Kedersha, NL, Fazikas, L, Streuli, M

EMBO J 1995
15750591 LAR receptor protein tyrosine phosphatases in the development and maintenance of excitatory synapses

Wyszynski, M, Jaworski, J, Sheng, M, Hueske, E, Dunah, AW, Simonetta, A, Hoogenraad, CC, Liu, G, Pak, DT

Nat. Neurosci. 2005
9624153 Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins

Serra-Pagès, C, Hart, A, Medley, QG, Streuli, M, Tang, M

J Biol Chem 1998
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