TY  - JOUR
A1  - Park, Misoon
A1  - Krause, Cornelia
A1  - Karnahl, Matthias
A1  - Reichardt, Ilka
A1  - El Kasmi, Farid
A1  - Mayer, Ulrike
A1  - Stierhof, York-Dieter
A1  - Hiller, Ulrike
A1  - Strompen, Georg
A1  - Bayer, Martin
A1  - Kientz, Marika
A1  - Sato, Masa H.
A1  - Nishimura, Marc T.
A1  - Dangl, Jeffery L.
A1  - Sanderfoot, Anton A.
A1  - Jürgens, Gerd
T1  - Concerted Action of Evolutionarily Ancient and Novel SNARE Complexes in Flowering-Plant Cytokinesis
JF  - Developmental cell
N2  - Membrane vesicles delivered to the cell-division plane fuse with one another to form the partitioning membrane during plant cytokinesis, starting in the cell center. In Arabidopsis, this requires SNARE complexes involving the cytokinesis-specific Qa-SNARE KNOLLE. However, cytokinesis still occurs in knolle mutant embryos, suggesting contributions from KNOLLE-independent SNARE complexes. Here we show that Qa-SNARE SYP132, having counterparts in lower plants, functionally overlaps with the flowering plant-specific KNOLLE. SYP132 mutation causes cytokinesis defects, knolle syp132 double mutants consist of only one or a few multi-nucleate cells, and SYP132 has the same SNARE partners as KNOLLE. SYP132 and KNOLLE also have non-overlapping functions in secretion and in cellularization of the embryo-nourishing endosperm resulting from double fertilization unique to flowering plants. Evolutionarily ancient non-specialized SNARE complexes originating in algae were thus amended by the appearance of cytokinesis-specific SNARE complexes, meeting the high demand for membrane-fusion capacity during endosperm cellularization in angiosperms.
Y1  - 2018
U6  - https://doi.org/10.1016/j.devcel.2017.12.027
SN  - 1534-5807
SN  - 1878-1551
VL  - 44
IS  - 4
SP  - 500
EP  - +
PB  - Cell Press
CY  - Cambridge
ER  - 
TY  - JOUR
A1  - Appelhagen, Ingo
A1  - Huep, Gunnar
A1  - Lu, Gui-Hua
A1  - Strompen, Georg
A1  - Weisshaar, Bernd
A1  - Sagasser, Martin
T1  - Weird fingers : functional analysis of WIP domain proteins
N2  - WIP proteins form a plant specific subfamily of C2H2 zinc finger (ZF) proteins. In this study, we functionally characterized the WIP domain, which consists of four ZF motifs, and discuss molecular functions for WIP proteins. Mutations in each of the ZFs lead to loss of function of the TT1/WIP1 protein in Arabiopsis thaliana. SV40 type nuclear localisation signals were detected in two of the ZFs and functionally characterized using GFP fusions as well as new mutant alleles identified by TILLING. Promoter swap experiments showed that selected WIP proteins are partially able to take over TT1 function. Activity of the AtBAN promoter, a potential TT1 target, could be increased by the addition of TT1 to the TT2-TT8-TTG1 regulatory complex.
Y1  - 2010
UR  - http://www.sciencedirect.com/science/journal/00145793
U6  - https://doi.org/10.1016/j.febslet.2010.06.007
SN  - 0014-5793
ER  -