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Nature 416, 178-183 (14 March 2002) | doi:10.1038/nature720; Received 30 November 2001; Accepted 22 January 2002; Published online 17 February 2002

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Drosophila Crumbs is a positional cue in photoreceptor adherens junctions and rhabdomeres

Shayan Izaddoost1, Sang-Chul Nam1, Manzoor A. Bhat2, Hugo J. Bellen1,3,4 & Kwang-Wook Choi1,3,5

  1. Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA
  2. Program in Developmental Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA
  3. Department of Molecular and Human Genetics, Howard Hughes Medical Institute, One Baylor Plaza, Houston, Texas 77030, USA
  4. Department of Ophthalmology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA
  5. Cardiovascular Research Institute, Department of Medicine, Department of Molecular Cell and Developmental Biology, Mount Sinai School of Medicine, New York, New York 10029, USA

Correspondence to: Kwang-Wook Choi1,3,5 Correspondence and requests for materials should be addressed to K.-W.C. (e-mail: Email: kchoi@bcm.tmc.edu).

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Drosophila Crumbs (Crb) is required for apical–basal polarity and is an apical determinant in embryonic epithelia1, 2. Here, we describe properties of Crb that control the position and integrity of the photoreceptor adherens junction and photosensitive organ, or rhabdomere3. In contrast to normal photoreceptor adherens junctions and rhabdomeres, which span the depth of the retina, adherens junctions and rhabdomeres of Crb-deficient photoreceptors initially accumulate at the top of the retina and fail to maintain their integrity as they stretch to the retinal floor. We show that Crb controls localization of the adherens junction through its intracellular domain containing a putative binding site for a protein 4.1 superfamily protein (FERM)4, 5. Although loss of Crb or overexpression of the FERM binding domain causes mislocalization of adherens junctions, they do not result in a significant loss of photoreceptor polarity. Mutations in CRB1, a human homologue of crb, are associated with photoreceptor degeneration in retinitis pigmentosa 12 (RP12) and Leber congenital amaurosis (LCA)6, 7, 8, 9, 10. The intracellular domain of CRB1 behaves similarly to its Drosophila counterpart when overexpressed in the fly eye. Our studies may provide clues for mechanisms of photoreceptor degeneration in RP12 and LCA.

  1. Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA
  2. Program in Developmental Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA
  3. Department of Molecular and Human Genetics, Howard Hughes Medical Institute, One Baylor Plaza, Houston, Texas 77030, USA
  4. Department of Ophthalmology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA
  5. Cardiovascular Research Institute, Department of Medicine, Department of Molecular Cell and Developmental Biology, Mount Sinai School of Medicine, New York, New York 10029, USA

Correspondence to: Kwang-Wook Choi1,3,5 Correspondence and requests for materials should be addressed to K.-W.C. (e-mail: Email: kchoi@bcm.tmc.edu).