Journal
EXPERIMENTAL CELL RESEARCH
Volume 265, Issue 2, Pages 329-338Publisher
ACADEMIC PRESS INC
DOI: 10.1006/excr.2001.5185
Keywords
FYVE domain; tyrosine phosphatase; phosphoinositide; localization; cloning; genomic structure
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Funding
- NCI NIH HHS [CA-68485, CA-75218] Funding Source: Medline
- NHLBI NIH HHS [HL-57393] Funding Source: Medline
- NIDDK NIH HHS [DK-15555, T32-DK07186] Funding Source: Medline
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We have recently isolated FYVE-DSP1, a FYVE domain-containing dual specificity protein phosphatase (R., Zhao, Y. Qi, and Z. J. Zhao, Biochem. Biophys. Res. Commun. 270, 222-229 (2000)). Here, we report a novel isozyme that we designated FYVE-DSP2. FYVE-2 contains a single FYVE domain at the C-terminus, and it shares similar to 47% overall sequence identity with FYBE-DSP1. Genomic sequence analyses revealed that the FYVE-DSP1 and FYVE-DSP2 genes share similar intron/exon organization, They are localized on human chromosome 22q12 and chromosome 17, respectively, Like FYVE-DBSP1, recombinant FYVE-DSP2 dephosphorylated low-molecular-weight phosphatase substrate para-nitrophenylphosphate, and its activity was inhibited by sodium vanadate. More importantly, our study also revealed that both FYVE-DSP1 and FYVE-DSP2 efficiently and specifically dephosphorylated phosphotidylinositol 3-phosphate. Subcellular fractionation demonstrated partition of FYVE-DSP1 and FYVE-DSP2 in membrane fractions, and. immunofluorescent cell staining showed perinuclear localization of the enzymes. FYVE-DSP2 is expressed in many human tissues with an alternatively spliced isoform expressed in the kidney. Together with two homologous hypothetical proteins found in Caenorhabditis elegans and Drosophila, FYVE-DSP1 and FYVE-DSP2 form a subfamily of phosphatases that may have an important role in cellular processes. (C) 2001 Academic Press.
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