Biochemical and Biophysical Research Communications
Regular ArticlecDNA Cloning of a Novel Protein Tyrosine Phosphatase with Homology to Cytoskeletal Protein 4.1 and Its Expression in T-Lineage Cells
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Protein tyrosine phosphatase PTPN14 Is a regulator of lymphatic function and choanal development in humans
2010, American Journal of Human GeneticsCitation Excerpt :These results were consistent with the hypothesis that VEGFC-mediated signaling may enhance the recruitment of PTPN14 to a protein complex that includes VEGFR3. The potential of these proteins to interact in vivo is also supported by independent work demonstrating that the expression patterns of Ptpn14 and Vegfr3 are broad and exhibit substantial overlap.25,34 The notion that PTPN14 might function in a multiprotein complex is further supported by the established role of its closest relative, PTPN21 (MIM 603271), which regulates proliferative signaling pathways through a scaffolding function.35,36
Localization of PTP-FERM in nerve processes through its FERM domain
2002, Biochemical and Biophysical Research CommunicationsComparative analysis of the Band 4.1/ezrin-related protein tyrosine phosphatase Pez from two Drosophila species: Implications for structure and function
2001, GeneCitation Excerpt :This potential interaction may be conserved, since Drosophila has two Eps8-related genes (based on BLAST analysis). Pro motif 3, PPPY, was also identified as an in vitro ligand for an Eps8 homolog (Mongiovi et al., 1999), and was previously noted as a potential SH3 ligand in mammalian forms of Pez (Sawada et al., 1994; Smith et al., 1995). Pro motifs 2, 4, and 5 may have arisen by duplication since they all share a consensus sequence: [neutral]-S-[N/Q/S/T]-P-[D/E]-[I/L/M/V] (dashes separate the residue positions; brackets indicate all allowed residues at one position).
Protein-tyrosine phosphatase D1, a potential regulator and effector for Tec family kinases
2000, Journal of Biological ChemistryCitation Excerpt :PTPD1 belongs to a group of cytosolic protein-tyrosine phosphatases containing an ezrin-like domain and a tyrosine phosphatase domain. This group of PTPs includes PTPH1 (69), PTPMEG (70), PTPBAS/PTP1E/PTPL1/FAP-1 (71), and PTPpez/PTP36 (54, 72, 73). Except for PTPBAS, which has an ezrin-like domain in the middle of the molecule, the other PTPs have the N-terminal ezrin-like domain and C-terminal PTP domain separated by an intervening sequence.
Regulation of mouse podocyte process dynamics by protein tyrosine phosphata ses
2000, Kidney InternationalCitation Excerpt :The cDNA reaction mix from RT minus reactions and water controls was consistently negative (data not shown). For detection of various PTPs, the following sequence-specific primers were designed according to published sequences17-22 and our own unpublished results: SHP-1: 5′,5′-GGGAATTCCCACCAGTGAGAGGTGG TACCA-3′ 3′,5′-CCCAAGCTTGAAGCAGGTAGACAAA GGCAC-3′