Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 52, Pages 18854-18859Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0509740102
Keywords
cell signaling; lysosome; phosphatidylinositol 5-phosphate
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Funding
- NHLBI NIH HHS [HL 16634, R01 HL016634, HL 55272] Funding Source: Medline
- NIAID NIH HHS [U54 AI057160] Funding Source: Medline
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Numerous inositol polyphosphate 5-phosphatases catalyze the degradation of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P-2) to phosphatidylinositol-4-phosphate (PtdIns-4-P). An alternative pathway to degrade PtdIns-4,5-P-2 is the hydrolysis of PtdIns-4,5-P-2 by a 4-phosphatase, leading to the production of PtdIns-5-P. Whereas the bacterial IpgD enzyme is known to catalyze this reaction, no such mammalian enzyme has been found. We have identified and characterized two previously undescribed human enzymes, PtdIns-4,5-P-2 4-phosphatase type I and type II, which catalyze the hydrolysis of PtdIns-4,5-P-2 to phosphatidylinositol-5-phosphate (PtdIns-5-P). Both enzymes are ubiquitously expressed and localize to late endosomal/lysosomal membranes in epithelial cells. Overexpression of either enzyme in HeLa cells increases EGF-receptor degradation upon EGF stimulation.
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