GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6

Wong, Siew Heng, Xu, Yue, Zhang, Tao, Griffiths, Gareth, Lowe, Stephen Loucian, Subramaniam, V. Nathan, Seow, Kah Tong and Hong, Wanjin (1999) GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6. Molecular Biology of The Cell, 10 1: 119-134.

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ222450_OA.pdf Full text (open access) application/pdf 1.18MB 0
Author Wong, Siew Heng
Xu, Yue
Zhang, Tao
Griffiths, Gareth
Lowe, Stephen Loucian
Subramaniam, V. Nathan
Seow, Kah Tong
Hong, Wanjin
Title GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
Publication date 1999-01
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 10
Issue 1
Start page 119
End page 134
Total pages 16
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Language eng
Abstract Syntaxin 1, synaptobrevins or vesicle-associated membrane proteins, and the synaptosome-associated protein of 25 kDa (SNAP-25) are key molecules involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. We report here the molecular, cell biological, and biochemical characterization of a 32-kDa protein homologous to both SNAP-25 (20% amino acid sequence identity) and the recently identified SNAP-23 (19% amino acid sequence identity). Northern blot analysis shows that the mRNA for this protein is widely expressed. Polyclonal antibodies against this protein detect a 32-kDa protein present in both cytosol and membrane fractions. The membrane-bound form of this protein is revealed to be primarily localized to the Golgi apparatus by indirect immunofluorescence microscopy, a finding that is further established by electron microscopy immunogold labeling showing that this protein is present in tubular-vesicular structures of the Golgi apparatus. Biochemical characterizations establish that this protein behaves like a SNAP receptor and is thus named Golgi SNARE of 32 kDa (GS32). GS32 in the Golgi extract is preferentially retained by the immobilized GST-syntaxin 6 fusion protein. The coimmunoprecipitation of syntaxin 6 but not syntaxin 5 or GS28 from the Golgi extract by antibodies against GS32 further sustains the preferential interaction of GS32 with Golgi syntaxin 6.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 54 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Thu, 25 Nov 2010, 10:34:14 EST