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First published online 1 November 2005
doi: 10.1242/jcs.02647

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Dishevelled (Dvl-2) activates canonical Wnt signalling in the absence of cytoplasmic puncta

¹ The Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK
² MRC Cell Biology Unit-LMCB, University College London, Gower Street, London, WC1E 6BT, UK
³ Improvision, Viscount Centre II, University of Warwick Science Park, Milburn Hill Road, Coventry, CV4 7HS, UK
⁴ CRC Centre for Cell and Molecular Biology, The Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK
⁵ Cardiff School of Biosciences, Biomedical Sciences Building, Museum Avenue, Cardiff, CF10 3US, UK

^* Author for correspondence (email: daletc{at}cardiff.ac.uk)

Accepted 15 August 2005

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.

Key words: Dishevelled, Dvl-2, endosomal, vesicle, Wnt

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