Abstract
Phosphoinositides (PIs) are phosphorylated derivatives of phosphatidylinositol (PtdIns) that regulate many cellular and physiological processes. Most PIs act by serving as membrane docking sites for proteins harboring specific PI-binding domains so that the location and function of these proteins could be dynamically governed. The Phox (PX) domain represents a novel PI-binding module capable of regulating membrane targeting of about 47 mammalian proteins, 30 of which are tentatively referred to as sorting nexins (SNXs). Some SNXs have been implicated in regulating membrane trafficking in the endocytic pathway. We discuss here recent development and progress in the study of the PX domain-containing proteins.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Carrier Proteins / physiology
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Cell Compartmentation
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Cell Membrane / metabolism*
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Humans
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Models, Biological
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Models, Molecular
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Molecular Sequence Data
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Phosphatidylinositol Phosphates
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Phosphatidylinositols / chemistry*
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Phosphatidylinositols / metabolism
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Phylogeny
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Protein Structure, Tertiary*
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Protein Transport
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Sorting Nexins
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Vacuoles / metabolism
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Vesicular Transport Proteins / chemistry*
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Vesicular Transport Proteins / genetics
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Vesicular Transport Proteins / metabolism*
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Vesicular Transport Proteins / physiology
Substances
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Carrier Proteins
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Phosphatidylinositol Phosphates
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Phosphatidylinositols
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Sorting Nexins
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Vesicular Transport Proteins