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First published online 20 September 2006
doi: 10.1242/dev.02563
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1 Section of Molecular Cell and Developmental Biology, Institute for Cellular
and Molecular Biology, University of Texas, Austin, TX 78712, USA.
2 Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA
15260, USA.
3 Institute for Neuroscience, University of Texas, Austin, TX 78712, USA.
Author for correspondence (e-mail:
wallingford{at}mail.utexas.edu)
Accepted 3 August 2006
Shroom family proteins have been implicated in the control of the actin
cytoskeleton, but so far only a single family member has been studied in the
context of developing embryos. Here, we show that the Shroom-family protein,
Shroom2 (previously known as APXL) is both necessary and sufficient to govern
the localization of pigment granules at the apical surface of epithelial
cells. In Xenopus embryos that lack Shroom2 function, we observed
defects in pigmentation of the eye that stem from failure of melanosomes to
mature and to associate with the apical cell surface. Ectopic expression of
Shroom2 in naïve epithelial cells facilitates apical pigment
accumulation, and this activity specifically requires the Rab27a GTPase. Most
interestingly, we find that Shroom2, like Shroom3 (previously called Shroom),
is sufficient to induce a dramatic apical accumulation of the
microtubule-nucleating protein
-tubulin at the apical surfaces of
naïve epithelial cells. Together, our data identify Shroom2 as a central
regulator of RPE pigmentation, and suggest that, despite their diverse
biological roles, Shroom family proteins share a common activity. Finally,
because the locus encoding human SHROOM2 lies within the critical region for
two distinct forms of ocular albinism, it is possible that SHROOM2
mutations may be a contributing factor in these human visual system
disorders.
Key words: Shroom, Shroom2, Retina, RPE, APXL, Melanosome, Ocular albinism
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