Abstract
Phosphoinositide signaling pathways regulate many essential cellular functions including proliferation, differentiation and survival, cytoskeletal organization, and vesicular trafficking. The inositol polyphosphate 5-phosphatases regulate the cellular levels of several bioactive phosphoinositide species. This review describes the structure and function of the 5-phosphatase and Sac1 catalytic domains of these enzymes. The crystal structure of the 5-phosphatase domain has been solved and shares homology with members of the AP endonuclease family. The phosphoinositide polyphosphatase activity of the Sac1 domain, found in some inositol polyphosphate 5-phosphatases, is defined by a motif, CX5 R(T/S), also found in both protein and lipid phosphatases.
MeSH terms
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Amino Acid Sequence
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Animals
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Carbon-Oxygen Lyases / chemistry
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Carbon-Oxygen Lyases / genetics
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Catalytic Domain
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DNA-(Apurinic or Apyrimidinic Site) Lyase
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Evolution, Molecular
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Humans
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Inositol Polyphosphate 5-Phosphatases
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Models, Molecular
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism
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Phosphoric Monoester Hydrolases / chemistry*
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Phosphoric Monoester Hydrolases / genetics
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Phosphoric Monoester Hydrolases / metabolism*
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Protein Structure, Tertiary
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Signal Transduction
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Substrate Specificity
Substances
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Nerve Tissue Proteins
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synaptojanin
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Phosphoric Monoester Hydrolases
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Inositol Polyphosphate 5-Phosphatases
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Carbon-Oxygen Lyases
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DNA-(Apurinic or Apyrimidinic Site) Lyase