A PTEN-related 5-Phosphatidylinositol Phosphatase Localized in the Golgi
Open accessAbstract
Phosphoinositides play important roles as signaling molecules in different cell compartments by regulating the localization and activity of proteins through their interaction with specific domains. The activity of these lipids depends on which sites on the inositol ring are phosphorylated. Signaling pathways dependent on phosphoinositides phosphorylated at the D3 position of this ring (3-phosphoinositides) are negatively regulated by 3-phosphoinositide-specific phosphatases that include PTEN and myotubularin. Using the conserved PTEN catalytic core motif, we have identified a new protein in the Dictyostelium genome called phospholipid-inositol phosphatase (PLIP), which defines a new subfamily of phosphoinositide phosphatases clearly distinct from PTEN or other closely related proteins. We show that PLIP is able to dephosphorylate a broad spectrum of phosphoinositides, including 3-phosphoinositides. In contrast to previously characterized phosphoinositide phosphatases, PLIP has a preference for phosphatidylinositol 5-phosphate, a newly discovered phosphoinositide. We found that PLIP is localized in the Golgi, with its phosphatase domain facing the cytoplasmic compartment. PLIP null cells created via homologous recombination are unable to effectively aggregate to form multicellular organisms at low cell densities. The presence of PLIP in the Golgi suggests that it may be involved in membrane trafficking.
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The product of plip is a phosphatidylinositol phosphatase with PI5P as preferential substrate.
“The product of the plip gene is also a phosphatidylinositol phosphatase with PI5P as preferential substrate [71].”
From Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium (2008) · cites this paper as [71]
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- Authors
- Merlot, S., Meili, R., Pagliarini, D. J., Maehama, T., Dixon, J. E., & Firtel, R. A.
- Affiliations
- University of California San Diego (US)
- University of Michigan (US)
- Corresponding author
- Firtel, Richard A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-10
- Volume
- 278
- Issue
- 41
- Pages
- 39866-39873
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2101225372
- Cited by
- 32
- References
- 53
- Citations by year
- 2024: 1 · 2022: 1 · 2020: 1 · 2018: 1 · 2014: 1 · 2013: 2 · 2012: 3
- FWCI
- 0.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- U.S. Public Health Service (18024)
- National Institute of General Medical Sciences (T32GM007752, 2 T32 GM07752-25)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- PLIP, PTEN, phosphoinositide phosphatase, phosphatidylinositol 5-phosphate, Golgi apparatus, Dictyostelium, phosphoinositide signaling, membrane trafficking, myotubularin
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Dictyostelium, Golgi Apparatus, Molecular Sequence Data, Phosphoric Monoester Hydrolases, RNA, Messenger, Protozoan Proteins, RNA, Protozoan, DNA, Protozoan, Gene Deletion, Sequence Homology, Amino Acid, Genome, Protozoan, Tumor Suppressor Proteins, PTEN Phosphohydrolase
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