PMID- 23515225
OWN - NLM
STAT- MEDLINE
DCOM- 20131223
LR  - 20221017
IS  - 1939-4586 (Electronic)
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 24
IP  - 10
DP  - 2013 May
TI  - SNARE complexes of different composition jointly mediate membrane fusion in 
      Arabidopsis cytokinesis.
PG  - 1593-601
LID - 10.1091/mbc.E13-02-0074 [doi]
AB  - Membrane fusion is mediated by soluble N-ethylmaleimide-sensitive factor 
      attachment protein receptor (SNARE) complexes. Although membrane fusion is 
      required for separating daughter cells in eukaryotic cytokinesis, the SNARE 
      complexes involved are not known. In plants, membrane vesicles targeted to the 
      cell division plane fuse with one another to form the partitioning membrane, 
      progressing from the center to the periphery of the cell. In Arabidopsis, the 
      cytokinesis-specific Qa-SNARE KNOLLE interacts with two other Q-SNAREs, SNAP33 
      and novel plant-specific SNARE 11 (NPSN11), whose roles in cytokinesis are not 
      clear. Here we show by coimmunoprecipitation that KNOLLE forms two SNARE 
      complexes that differ in composition. One complex is modeled on the trimeric 
      plasma membrane type of SNARE complex and includes, in addition to KNOLLE, the 
      promiscuous Qb,c-SNARE SNAP33 and the R-SNARE vesicle-associated membrane protein 
      (VAMP) 721,722, also involved in innate immunity. In contrast, the other 
      KNOLLE-containing complex is tetrameric and includes Qb-SNARE NPSN11, Qc-SNARE 
      SYP71, and VAMP721,722. Elimination of only one or the other type of KNOLLE 
      complex by mutation, including the double mutant npsn11 syp71, causes a mild or 
      no cytokinesis defect. In contrast, the two double mutants snap33 npsn11 and 
      snap33 syp71 eliminate both types of KNOLLE complexes and display knolle-like 
      cytokinesis defects. Thus the two distinct types of KNOLLE complexes appear to 
      jointly mediate membrane fusion in Arabidopsis cytokinesis.
FAU - El Kasmi, Farid
AU  - El Kasmi F
AD  - Developmental Genetics, Center for Plant Molecular Biology, University of 
      Tubingen, 72076 Tubingen, Germany.
FAU - Krause, Cornelia
AU  - Krause C
FAU - Hiller, Ulrike
AU  - Hiller U
FAU - Stierhof, York-Dieter
AU  - Stierhof YD
FAU - Mayer, Ulrike
AU  - Mayer U
FAU - Conner, Laura
AU  - Conner L
FAU - Kong, Lingtian
AU  - Kong L
FAU - Reichardt, Ilka
AU  - Reichardt I
FAU - Sanderfoot, Anton A
AU  - Sanderfoot AA
FAU - Jurgens, Gerd
AU  - Jurgens G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130320
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (KNOLLE protein, Arabidopsis)
RN  - 0 (NPSN11 protein, Arabidopsis)
RN  - 0 (Qa-SNARE Proteins)
RN  - 0 (Qb-SNARE Proteins)
RN  - 0 (Qc-SNARE Proteins)
RN  - 0 (R-SNARE Proteins)
RN  - 0 (SNAP33 protein, Arabidopsis)
RN  - 0 (VAMP721 protein, Arabidopsis)
RN  - 0 (VAMP722 protein, Arabidopsis)
SB  - IM
MH  - Arabidopsis/cytology/*metabolism
MH  - Arabidopsis Proteins/genetics/*metabolism
MH  - *Cytokinesis
MH  - *Membrane Fusion
MH  - Protein Interaction Mapping
MH  - Protein Transport
MH  - Qa-SNARE Proteins/*metabolism
MH  - Qb-SNARE Proteins/genetics/*metabolism
MH  - Qc-SNARE Proteins/genetics/*metabolism
MH  - R-SNARE Proteins/metabolism
PMC - PMC3655819
EDAT- 2013/03/22 06:00
MHDA- 2013/12/24 06:00
PMCR- 2013/07/30
CRDT- 2013/03/22 06:00
PHST- 2013/03/22 06:00 [entrez]
PHST- 2013/03/22 06:00 [pubmed]
PHST- 2013/12/24 06:00 [medline]
PHST- 2013/07/30 00:00 [pmc-release]
AID - mbc.E13-02-0074 [pii]
AID - E13-02-0074 [pii]
AID - 10.1091/mbc.E13-02-0074 [doi]
PST - ppublish
SO  - Mol Biol Cell. 2013 May;24(10):1593-601. doi: 10.1091/mbc.E13-02-0074. Epub 2013 
      Mar 20.