title: Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins.
abstract: LAR family transmembrane protein-tyrosine phosphatases function in axon guidance and mammary gland development. In cultured cells, LAR binds to the intracellular, coiled coil LAR-interacting protein at discrete ends of focal adhesions, implicating these proteins in the regulation of cell-matrix interactions. We describe seven LAR-interacting protein-like genes in humans and Caenorhabditis elegans that form the liprin gene family. 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. Both alpha- and beta-liprins homodimerize via their N-terminal, coiled coil regions. Liprins are thus multivalent proteins that potentially form complex structures. Some liprins have broad mRNA tissue distributions, whereas others are predominately expressed in the brain. Co-expression studies indicate that liprin-alpha2 alters LAR cellular localization and induces LAR clustering. We propose that liprins function to localize LAR family tyrosine phosphatases at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.
authors.affiliation: Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.
authors.forename: C
authors.initials: C
authors.lastname: Serra-Pagès
authors.forename: Q G
authors.initials: QG
authors.lastname: Medley
authors.forename: M
authors.initials: M
authors.lastname: Tang
authors.forename: A
authors.initials: A
authors.lastname: Hart
authors.forename: M
authors.initials: M
authors.lastname: Streuli
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000235:genetics*; D019143:Evolution, Molecular; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D005810:Multigene Family; D010750:Phosphoproteins / Q000737:chemistry / Q000235:genetics*; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D054630:Receptor-Like Protein Tyrosine Phosphatases, Class 4; D011956:Receptors, Cell Surface
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D029742:Caenorhabditis elegans Proteins; D015815:Cell Adhesion Molecules; D036341:Intercellular Signaling Peptides and Proteins; C094398:PPFIA1 protein, human; D010750:Phosphoproteins; D012333:RNA, Messenger; D011956:Receptors, Cell Surface; C490598:SYD-2 protein, C elegans; C516841:PTPRA protein, human; D017027:Protein Tyrosine Phosphatases; D054630:Receptor-Like Protein Tyrosine Phosphatases, Class 4