Abstract
Postsynaptic targeting of PSD-95 has been extensively studied; however, little is known about how other MAGUKs are localized. Proper targeting of PSD-95 requires dual palmitoylation of an N-terminal motif. We now find that the N-termini of closely related PSD-93 and SAP-102 are also involved in postsynaptic targeting. PSD-93 is N-terminally palmitoylated; however, unlike PSD-95, palmitoylation does not explain the necessity of the N-terminus for PSD-93 postsynaptic targeting. Furthermore, when the N-terminus of PSD-95 is replaced with the first 30 or 64, but not the first 10, amino acids of PSD-93, the chimera is targeted to postsynaptic sites independent of palmitoylation. Similarly, when the N-terminus of PSD-95 is replaced with the non-palmitoylated N-terminus of SAP-102, postsynaptic targeting is maintained. These results suggest that MAGUKs contain diverse signals within their N-termini for postsynaptic targeting.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Cells, Cultured
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Disks Large Homolog 4 Protein
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Embryo, Mammalian
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Guanylate Kinases
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Hippocampus / cytology
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Hippocampus / physiology
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / metabolism*
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Neurons / cytology
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Neurons / physiology*
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Neuropeptides / chemistry
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Neuropeptides / metabolism*
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Nucleoside-Phosphate Kinase / metabolism*
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Palmitic Acid / metabolism
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Rats
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Synapses / physiology*
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Synapses / ultrastructure
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Transfection
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Tumor Suppressor Proteins
Substances
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Disks Large Homolog 4 Protein
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Dlg3 protein, rat
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Dlg4 protein, rat
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Mpp2 protein, rat
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Nerve Tissue Proteins
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Neuropeptides
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Recombinant Proteins
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Tumor Suppressor Proteins
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postsynaptic density proteins
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Palmitic Acid
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Nucleoside-Phosphate Kinase
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DLG2 protein, human
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Guanylate Kinases