Abstract
Dishevelled family proteins are multidomain intracellular transducers of Wnt signals. Ectopically expressed mammalian Dishevelled 2 (Dvl-2) activates downstream signalling and localises to cytoplasmic puncta. It has been suggested that these Dvl-2-containing structures correspond to intracellular vesicles and may be involved in the Wnt signal transduction process. We report that cytoplasmic puncta are primarily formed in cells expressing Dvl-2 at high levels. Lower levels of expression can activate signalling without forming puncta. The structures do not localise with markers of the early or late endocytic pathway and time-lapse analysis demonstrates that Dvl-2 puncta move in a random fashion over short distances but do not originate from the plasma membrane. Based on our findings, we propose that Dvl-2 puncta are protein aggregates that are not required for signalling.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Animals
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Antigens, CD / metabolism
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Biomarkers / analysis
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Cricetinae
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Cytoplasm / metabolism*
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Dishevelled Proteins
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Dogs
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Endocytosis
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Endoplasmic Reticulum / metabolism
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Humans
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Membrane Proteins / metabolism
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Phosphoproteins / chemistry
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Phosphoproteins / genetics
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Phosphoproteins / metabolism*
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Platelet Membrane Glycoproteins / metabolism
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Protein Binding
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Protein Structure, Tertiary
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Protein Transport
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Signal Transduction* / drug effects
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Tetraspanin 30
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Time Factors
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Transfection
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Vesicular Transport Proteins
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Wnt Proteins / metabolism*
Substances
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Adaptor Proteins, Signal Transducing
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Antigens, CD
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Biomarkers
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CD63 protein, human
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DVL2 protein, human
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Dishevelled Proteins
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Membrane Proteins
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Phosphoproteins
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Platelet Membrane Glycoproteins
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Tetraspanin 30
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Vesicular Transport Proteins
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Wnt Proteins
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early endosome antigen 1