Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells
Open accessAbstract
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).”
From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Beronja et al, 2005
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Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst
Teodoro, R. O., Pekkurnaz, G., Nasser, A., Higashi‐Kovtun, M. E., Balakireva, M., McLachlan, I. G., Camonis, J., & Schwarz, T. L. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.147 · Cited by 61 · see citing works
- 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
- Publisher
- Rockefeller University Press
- Published
- 2005-05-16
- Volume
- 169
- Issue
- 4
- Pages
- 635-646
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2171699
- OpenAlex
- W2073745779
- Cited by
- 120
- References
- 0
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 2 · 2016: 9 · 2015: 8 · 2014: 3 · 2013: 7 · 2012: 7
- FWCI
- 3.93
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- 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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