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PMID: 11739776 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Interactions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell.

Molecular biology of the cell ·Vol. 12 ·No. 12 ·2001-12-00 ·Pages 3733-43

Sanderfoot AA, Kovaleva V, Bassham DC, Raikhel NV

Abstract

The syntaxin family of soluble N-ethyl maleimide sensitive factor adaptor protein receptors (SNAREs) is known to play an important role in the fusion of transport vesicles with specific organelles. Twenty-four syntaxins are encoded in the genome of the model plant Arabidopsis thaliana. These 24 genes are found in 10 gene families and have been reclassified as syntaxins of plants (SYPs). Some of these gene families have been previously characterized, with the SYP2-type syntaxins being found in the prevacuolar compartment (PVC) and the SYP4-type syntaxins on the trans-Golgi network (TGN). Here we report on two previously uncharacterized syntaxin groups. The SYP5 group is encoded by a two-member gene family, whereas SYP61 is a single gene. Both types of syntaxins are localized to multiple compartments of the endomembrane system, including the TGN and the PVC. These two groups of syntaxins form SNARE complexes with each other, and with other Arabidopsis SNAREs. On the TGN, SYP61 forms complexes with the SNARE VTI12 and either SYP41 or SYP42. SYP51 and SYP61 interact with each other and with VTI12, most likely also on the TGN. On the PVC, a SYP5-type syntaxin interacts specifically with a SYP2-type syntaxin, as well as the SNARE VTI11, forming a SNARE complex likely involved in TGN-to-PVC trafficking.

MeSH Terms
Amino Acid Sequence Arabidopsis/cytology,metabolism,ultrastructure Arabidopsis Proteins/metabolism Biological Transport, Active Cloning, Molecular Golgi Apparatus/chemistry,metabolism Intracellular Membranes/metabolism Macromolecular Substances Membrane Proteins/chemistry,metabolism Microscopy, Electron Molecular Sequence Data Protein Binding Protein Structure, Tertiary Qa-SNARE Proteins Reverse Transcriptase Polymerase Chain Reaction SNARE Proteins Sequence Alignment Vesicular Transport Proteins trans-Golgi Network/chemistry,metabolism
Chemicals
Arabidopsis Proteins Macromolecular Substances Membrane Proteins Qa-SNARE Proteins SNARE Proteins Vesicular Transport Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sanderfoot A A
Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824-1312, USA.
Kovaleva V
Bassham D C
Raikhel N V
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
2001-12-00
Pages
3733-43
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC60751
Subset
IM
Grants
NIGMS NIH HHS · F32 GM018861 · United States
NIGMS NIH HHS · GM-18861 · United States
Databases
GENBANK
AF355754, AF355755, AF355756, AF355757, AF355758, AF355759
Corrections
ErratumIn
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