Cited by 120Cellular transport and secretionExtracellular vesicles in diseaseDevelopmental Biology and Gene Regulation

Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells

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Beronja, Slobodan, Laprise, Patrick, Papoulas, Ophelia, Pellikka, Milena, Sisson, John, Tepass, Ulrich·2005·The Journal of Cell Biology

Abstract

Polarized exocytosis plays a major role in development and cell differentiation but the mechanisms that target exocytosis to specific membrane domains in animal cells are still poorly understood. We characterized Drosophila Sec6, a component of the exocyst complex that is believed to tether secretory vesicles to specific plasma membrane sites. sec6 mutations cause cell lethality and disrupt plasma membrane growth. In developing photoreceptor cells (PRCs), Sec6 but not Sec5 or Sec8 shows accumulation at adherens junctions. In late PRCs, Sec6, Sec5, and Sec8 colocalize at the rhabdomere, the light sensing subdomain of the apical membrane. PRCs with reduced Sec6 function accumulate secretory vesicles and fail to transport proteins to the rhabdomere, but show normal localization of proteins to the apical stalk membrane and the basolateral membrane. Furthermore, we show that Rab11 forms a complex with Sec5 and that Sec5 interacts with Sec6 suggesting that the exocyst is a Rab11 effector that facilitates protein transport to the apical rhabdomere in Drosophila PRCs.

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  • The distribution of the exocyst within a cell can be highly dynamic, consistent with its role in directing membrane fusion to specific domains.

    “The distribution of the exocyst within a cell can be highly dynamic, consistent with its role in directing membrane fusion to specific domains (Boyd et al, 2004;Beronja et al, 2005;Mehta et al, 2005;Zhang et al, 2008;Murthy et al, 2010).”

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Authors
Beronja, S., Laprise, P., Papoulas, O., Pellikka, M., Sisson, J., & Tepass, U.
Affiliations
  • University of Toronto (CA)
  • The University of Texas at Austin (US)
Corresponding author
Tepass, Ulrich
Venue
The Journal of Cell Biology
Published
2005-05-16
Volume
169
Issue
4
Pages
635-646
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2073745779
Cited by
120
References
0
Citations by year
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FWCI
3.93
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
National Institute of General Medical Sciences (GM 067013, R01GM067013)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords
Sec6, exocyst complex, polarized exocytosis, photoreceptors, rhabdomere, Rab11, secretory vesicle transport, adherens junctions, Sec5, Sec8, Drosophila
MeSH terms
rab11 GTP-Binding Proteins, Amino Acid Sequence, Animals, Base Sequence, Cell Membrane, Drosophila melanogaster, Epithelial Cells, Exocytosis, Eye, Female, Germ Cells, Larva, Membrane Proteins, Molecular Sequence Data, Mutation, Photoreceptor Cells, Invertebrate, rab GTP-Binding Proteins, Protein Transport, Adherens Junctions, Secretory Vesicles, Drosophila Proteins, Vesicular Transport Proteins, Microscopy, Electron, Transmission

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