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The 67 kDa laminin receptor (67LR) is a non-integrin cell surface receptor encoded by the RPSA gene, which also functions as a component of the 40S ribosomal subunit (UniProt P08865). It is formed through the post-translational modification or dimerization of a 37 kDa precursor (37LRP) and is ubiquitously expressed in mammalian tissues. 67LR is a primary attachment receptor for Adeno-associated virus serotype 9 (AAV9), a vector widely used in gene therapy for its ability to cross the blood-brain barrier (Akache et al., 2006, J. Virol.). AAV9 entry is a multi-step process that also involves terminal N-linked galactose residues for initial docking and the Adeno-associated virus receptor (AAVR/KIAA0319L) for subsequent endosomal trafficking (Pillay et al., 2016, Nature; Shen et al., 2011, J. Biol. Chem.). In addition to its role in viral entry, 67LR is frequently overexpressed in various cancers, where it correlates with increased metastatic potential and poor prognosis by modulating cell adhesion and migration (Nelson et al., 2008, Cancer Lett.). It also serves as a receptor for the green tea polyphenol EGCG and has been implicated in the internalization of pathogenic prion proteins and amyloid-beta peptides, suggesting a role in neurodegenerative diseases.
Acts as a high-affinity cell surface receptor for viral attachment and internalization, specifically for AAV9; also mediates cell-extracellular matrix adhesion by binding to laminin-1.
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