Abstract
As a tetramer, acetylcholinesterase (AChE) is anchored to the basal lamina of the neuromuscular junction and to the membrane of neuronal synapses. We have previously shown that collagen Q (ColQ) anchors AChE at the neuromuscular junction. We have now cloned the gene PRiMA (proline-rich membrane anchor) encoding the AChE anchor in mammalian brain. We show that PRiMA is able to organize AChE into tetramers and to anchor them at the surface of transfected cells. Furthermore, we demonstrate that AChE is actually anchored in neural cell membranes through its interaction with PRiMA. Finally, we propose that only PRiMA anchors AChE in mammalian brain and muscle cell membranes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylcholinesterase / chemistry
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Acetylcholinesterase / metabolism*
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Animals
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Brain / enzymology*
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Butyrylcholinesterase / chemistry
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Cell Membrane / enzymology
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Cell Membrane / metabolism
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Collagen / chemistry
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DNA, Complementary / genetics
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / physiology*
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Mice
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Molecular Sequence Data
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Muscle Proteins*
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Muscle, Skeletal / enzymology
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / physiology*
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Oocytes
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Proline
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Protein Structure, Tertiary
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Tumor Cells, Cultured
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Xenopus
Substances
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DNA, Complementary
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Membrane Proteins
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Muscle Proteins
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Nerve Tissue Proteins
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prima1 protein, mouse
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Collagen
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Proline
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Acetylcholinesterase
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COLQ protein, human
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Butyrylcholinesterase