Update on plant cytokinesis: rule and divide

2019 ◽  
Vol 52 ◽  
pp. 97-105 ◽  
Author(s):  
Henrik Buschmann ◽  
Sabine Müller
Keyword(s):  
2011 ◽  
Vol 21 (22) ◽  
pp. R926-R927 ◽  
Author(s):  
Clive Lloyd
Keyword(s):  

2018 ◽  
Author(s):  
Han Tang ◽  
Jeroen de Keijzer ◽  
Elysa Overdijk ◽  
Els Sweep ◽  
Maikel Steentjes ◽  
...  

AbstractDuring plant cytokinesis a radially expanding membrane-enclosed cell plate is formed from fusing vesicles that compartmentalizes the cell in two. How fusion is spatially restricted to the site of cell plate formation is unknown. Aggregation of cell-plate membrane starts near regions of microtubule overlap within the bipolar phragmoplast apparatus of the moss Physcomitrella patens. Since vesicle fusion generally requires coordination of vesicle tethering and subsequent fusion activity we analysed the subcellular localization of several subunits of the exocyst, a tethering complex active during plant cytokinesis. We found that Sec6, but neither Sec3 or Sec5 subunits localized to microtubule overlap regions in advance of cell plate construction started in moss. Moreover, Sec6 exhibited a conserved physical interaction with an orthologue of the Sec1/Munc18 protein KEULE, an important regulator for cell-plate membrane vesicle fusion in Arabidopsis. Recruitment of PpKEULE and vesicles to the early cell plate was delayed upon Sec6 gene silencing. Our findings thus suggest that vesicle-vesicle fusion is in part enabled by a pool of exocyst subunits at microtubule overlaps that is recruited independent of the delivery of vesicles.Summary statementWe performed a time-resolved localization screen of multiple subunits of the exocyst complex throughout moss cytokinesis and show that each subunit has a unique spatiotemporal recruitment pattern.


Author(s):  
M. Sasabe ◽  
Y. Takahashi ◽  
T. Soyano ◽  
H. Tanaka ◽  
K. Kousetsu ◽  
...  

2016 ◽  
Vol 88 (4) ◽  
pp. 531-541 ◽  
Author(s):  
Alexander Steiner ◽  
Katarzyna Rybak ◽  
Melina Altmann ◽  
Heather E. McFarlane ◽  
Susan Klaeger ◽  
...  

PROTOPLASMA ◽  
2016 ◽  
Vol 254 (1) ◽  
pp. 569-586 ◽  
Author(s):  
Pantelis Livanos ◽  
Basil Galatis ◽  
Hartmut Quader ◽  
Panagiotis Apostolakos

Traffic ◽  
2002 ◽  
Vol 3 (9) ◽  
pp. 621-629 ◽  
Author(s):  
Sebastian Y. Bednarek ◽  
Tanya G. Falbel

2001 ◽  
Vol 155 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Maren Heese ◽  
Xavier Gansel ◽  
Liliane Sticher ◽  
Peter Wick ◽  
Markus Grebe ◽  
...  

Cytokinesis requires membrane fusion during cleavage-furrow ingression in animals and cell plate formation in plants. In Arabidopsis, the Sec1 homologue KEULE (KEU) and the cytokinesis-specific syntaxin KNOLLE (KN) cooperate to promote vesicle fusion in the cell division plane. Here, we characterize AtSNAP33, an Arabidopsis homologue of the t-SNARE SNAP25, that was identified as a KN interactor in a yeast two-hybrid screen. AtSNAP33 is a ubiquitously expressed membrane-associated protein that accumulated at the plasma membrane and during cell division colocalized with KN at the forming cell plate. A T-DNA insertion in the AtSNAP33 gene caused loss of AtSNAP33 function, resulting in a lethal dwarf phenotype. atsnap33 plantlets gradually developed large necrotic lesions on cotyledons and rosette leaves, resembling pathogen-induced cellular responses, and eventually died before flowering. In addition, mutant seedlings displayed cytokinetic defects, and atsnap33 in combination with the cytokinesis mutant keu was embryo lethal. Analysis of the Arabidopsis genome revealed two further SNAP25-like proteins that also interacted with KN in the yeast two-hybrid assay. Our results suggest that AtSNAP33, the first SNAP25 homologue characterized in plants, is involved in diverse membrane fusion processes, including cell plate formation, and that AtSNAP33 function in cytokinesis may be replaced partially by other SNAP25 homologues.


2006 ◽  
Vol 10 (1) ◽  
pp. 137-150 ◽  
Author(s):  
Pankaj Dhonukshe ◽  
František Baluška ◽  
Markus Schlicht ◽  
Andrej Hlavacka ◽  
Jozef Šamaj ◽  
...  

1980 ◽  
Vol 20 (4) ◽  
pp. 455-461 ◽  
Author(s):  
A. Gonzalez-Fernandez ◽  
J.F. Lopez-Saez
Keyword(s):  

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Sandra Richter ◽  
Marika Kientz ◽  
Sabine Brumm ◽  
Mads Eggert Nielsen ◽  
Misoon Park ◽  
...  

Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1–BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell–division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint.


Sign in / Sign up

Export Citation Format

Share Document