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Research Article
The roles of Syx5 in Golgi morphology and Rhodopsin transport in Drosophila photoreceptors
Takunori Satoh, Yuri Nakamura, Akiko K. Satoh
Biology Open 2016 5: 1420-1430; doi: 10.1242/bio.020958
Takunori Satoh
Division of Life Science, Graduate School of Integral Arts and Science, Hiroshima University, 1-7-1, Kagamiyama, Higashi-hiroshima 739-8521, Japan
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Yuri Nakamura
Division of Life Science, Graduate School of Integral Arts and Science, Hiroshima University, 1-7-1, Kagamiyama, Higashi-hiroshima 739-8521, Japan
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Akiko K. Satoh
Division of Life Science, Graduate School of Integral Arts and Science, Hiroshima University, 1-7-1, Kagamiyama, Higashi-hiroshima 739-8521, Japan
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  • ORCID record for Akiko K. Satoh
  • For correspondence: aksatoh@hiroshima-u.ac.jp
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ABSTRACT

SNAREs (SNAP receptors) are the key components of protein complexes that drive membrane fusion. Here, we report the function of a SNARE, Syntaxin 5 (Syx5), in the development of photoreceptors in Drosophila. In wild-type photoreceptors, Syx5 localizes to cis-Golgi, along with cis-Golgi markers: Rab1 and GM130. We observed that Syx5-deficient photoreceptors show notable accumulation of these cis-Golgi markers accompanying drastic accumulation of vesicles between endoplasmic reticulum (ER) and Golgi cisternae. Extensive analysis of Rh1 (rhodopsin 1) trafficking revealed that in Syx5-deficient photoreceptors, Rh1 is exported from the ER with normal kinetics, retained in the cis-Golgi region along with GM130 for a prolonged period, and then subsequently degraded presumably by endoplasmic reticulum-associated protein degradation (ERAD) after retrieval to the ER. Unlike our previous report of Rab6-deficient photoreceptors – where two apical transport pathways are specifically inhibited – vesicle transport pathways to all plasma membrane domains are inhibited in Syx5-deficient photoreceptors, implying that Rab6 and Syx5 are acting in different steps of intra-Golgi transport. These results indicate that Syx5 is crucial for membrane protein transport, presumably during ER-derived vesicle fusion to form cis-Golgi cisternae.

Footnotes

  • Competing interests

    The authors declare no competing or financial interests.

  • Author contributions

    T.S., A.K.S. conception and design, acquisition of data, analysis and interpretation of data, drafting and revising of the article; Y.N. acquisition of data, analysis and interpretation of data, drafting and revising the article.

  • Funding

    This work was supported by Precursory Research for Embryonic Science and Technology [grant no. 25-J-J4215 to A.K.S.], KAKENHI [grant no. 15K07050 to A.K.S.].

  • Supplementary information

    Supplementary information available online at http://bio.biologists.org/lookup/doi/10.1242/bio.020958.supplemental

  • Received July 27, 2016.
  • Accepted August 25, 2016.
  • © 2016. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Keywords

  • Syx5
  • Rhodopsin
  • ER
  • Golgi
  • Vesicle cluster

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Research Article
The roles of Syx5 in Golgi morphology and Rhodopsin transport in Drosophila photoreceptors
Takunori Satoh, Yuri Nakamura, Akiko K. Satoh
Biology Open 2016 5: 1420-1430; doi: 10.1242/bio.020958
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Research Article
The roles of Syx5 in Golgi morphology and Rhodopsin transport in Drosophila photoreceptors
Takunori Satoh, Yuri Nakamura, Akiko K. Satoh
Biology Open 2016 5: 1420-1430; doi: 10.1242/bio.020958

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