TY - JOUR
T1 - VAMP4 and its cognate SNAREs are required for maintaining the ribbon structure of the Golgi apparatus
AU - Shitara, Akiko
AU - Shibui, Toru
AU - Okayama, Miki
AU - Arakawa, Toshiya
AU - Mizoguchi, Itaru
AU - Sakakura, Yasunori
AU - Takuma, Taishin
N1 - Publisher Copyright:
© 2017 Japanese Association for Oral Biology
PY - 2017/11
Y1 - 2017/11
N2 - Background The Golgi apparatus is at a crossroads between anterograde and retrograde trafficking. It exhibits a twisted ribbon-like network in the juxtanuclear region of vertebrate cells. Vesicle-associated membrane protein 4 (VAMP4) is a unique v-SNARE expressed exclusively in trans-Golgi networks (TGN), where it regulates retrograde trafficking from the early endosome to the TGN with its cognate SNARE partners Syntaxin 6, Syntaxin 16, and Vti1a. Highlight To examine whether VAMP4 plays a role in maintaining the Golgi ribbon structure, we depleted VAMP4 expression using a small interfering RNA. Depletion of VAMP4 led to fragmentation of the Golgi ribbon in HeLa cells. Immunohistochemical analysis showed that, in the absence of VAMP4, although the Golgi stack length was shortened, Golgi stacking was normal. Furthermore, depletion of the cognate SNARE partners of VAMP4 also disrupted the Golgi ribbon structure. Microscopy-based analyses showed that Golgi fragmentation did not impair anterograde traffic. Conclusion Our findings suggest that VAMP4 and its cognate SNAREs are required for maintaining the Golgi ribbon structure by balancing membrane transport between the endosome and TGN.
AB - Background The Golgi apparatus is at a crossroads between anterograde and retrograde trafficking. It exhibits a twisted ribbon-like network in the juxtanuclear region of vertebrate cells. Vesicle-associated membrane protein 4 (VAMP4) is a unique v-SNARE expressed exclusively in trans-Golgi networks (TGN), where it regulates retrograde trafficking from the early endosome to the TGN with its cognate SNARE partners Syntaxin 6, Syntaxin 16, and Vti1a. Highlight To examine whether VAMP4 plays a role in maintaining the Golgi ribbon structure, we depleted VAMP4 expression using a small interfering RNA. Depletion of VAMP4 led to fragmentation of the Golgi ribbon in HeLa cells. Immunohistochemical analysis showed that, in the absence of VAMP4, although the Golgi stack length was shortened, Golgi stacking was normal. Furthermore, depletion of the cognate SNARE partners of VAMP4 also disrupted the Golgi ribbon structure. Microscopy-based analyses showed that Golgi fragmentation did not impair anterograde traffic. Conclusion Our findings suggest that VAMP4 and its cognate SNAREs are required for maintaining the Golgi ribbon structure by balancing membrane transport between the endosome and TGN.
KW - Golgi fragmentation
KW - Golgi ribbon architecture
KW - Membrane transport
KW - SNARE
KW - VAMP4
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U2 - 10.1016/j.job.2017.05.005
DO - 10.1016/j.job.2017.05.005
M3 - Review article
AN - SCOPUS:85021116054
SN - 1349-0079
VL - 59
SP - 192
EP - 196
JO - Journal of Oral Biosciences
JF - Journal of Oral Biosciences
IS - 4
ER -