TY  - JOUR
A1  - Blasig, Ingolf E.
A1  - Winkler, Lars
A1  - Lassowski, Birgit
A1  - Müller, Sandra L.
A1  - Zuleger, Nikolaj
A1  - Krause, Eberhard
A1  - Krause, Gerd
A1  - Gast, Klaus
A1  - Kolbe, Michael
A1  - Piontek, Jörg
T1  - On the self-association potential of transmembrane tight junction proteins
N2  - Tight junctions seal intercellular clefts via membrane-related strands, hence, maintaining important organ functions. We investigated the self-association of strand-forming transmembrane tight junction proteins. The regulatory tight junction protein occludin was differently tagged and cotransfected in eucaryotic cells. These occludins colocalized within the plasma membrane of the same cell, coprecipitated and exhibited fluorescence resonance energy transfer. Differently tagged strand-forming claudin-5 also colocalized in the plasma membrane of the same cell and showed fluorescence resonance energy transfer. This demonstrates self-association in intact cells both of occludin and claudin-5 in one plasma membrane. In search of dimerizing regions of occludin, dimerization of its cytosolic C-terminal coiled-coil domain was identified. In claudin-5, the second extracellular loop was detected as a dimer. Since the transmembrane junctional adhesion molecule also is known to dimerize, the assumption that homodimerization of transmembrane tight junction proteins may serve as a common structural feature in tight junction assembly is supported
Y1  - 2006
UR  - http://www.springerlink.com/content/101193
U6  - https://doi.org/10.1007/s00018-005-5472-x
SN  - 1420-682X
ER  - 
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  -