Downloads: 78

Files in This Item:
File Description SizeFormat 
bio.012146.pdf1.89 MBAdobe PDFView/Open
Title: SNAP23/25 and VAMP2 mediate exocytic event of transferrin receptor-containing recycling vesicles
Authors: Kubo, Keiji
Kobayashi, Minako
Nozaki, Shohei
Yagi, Chikako
Hatsuzawa, Kiyotaka
Katoh, Yohei  kyouindb  KAKEN_id  orcid (unconfirmed)
Shin, Hye-Won  kyouindb  KAKEN_id  orcid (unconfirmed)
Takahashi, Senye
Nakayama, Kazuhisa  kyouindb  KAKEN_id  orcid (unconfirmed)
Keywords: SNAP23
Recycling endosome
Transferrin receptor
Issue Date: Jun-2015
Publisher: The Company of Biologists
Journal title: Biology open
Volume: 4
Start page: 910
End page: 920
Abstract: We recently showed that Rab11 is involved not only in formation of recycling vesicles containing the transferrin (Tfn)–transferrin receptor (TfnR) complex at perinuclear recycling endosomes but also in tethering of recycling vesicles to the plasma membrane (PM) in concert with the exocyst tethering complex. We here aimed at identifying SNARE proteins responsible for fusion of Tfn–TfnR-containing recycling vesicles with the PM, downstream of the exocyst. We showed that exocyst subunits, Sec6 and Sec8, can interact with SNAP23 and SNAP25, both of which are PM-localizing Q[bc]-SNAREs, and that depletion of SNAP23 and/or SNAP25 in HeLa cells suppresses fusion of Tfn–TfnR-containing vesicles with the PM, leading to accumulation of the vesicles at the cell periphery. We also found that VAMP2, an R-SNARE, is colocalized with endocytosed Tfn on punctate endosomal structures, and that its depletion in HeLa cells suppresses recycling vesicle exocytosis. These observations indicate that fusion of recycling vesicles with the PM downstream of the exocyst is mediated by SNAP23/25 and VAMP2, and provide novel insight into non-neuronal roles of VAMP2 and SNAP25.
Rights: This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
DOI(Published Version): 10.1242/bio.012146
PubMed ID: 26092867
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks

Export Format: 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.