scholarly journals ER assembly of SNARE complexes mediating formation of partitioning membrane in Arabidopsis cytokinesis

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Matthias Karnahl ◽  
Misoon Park ◽  
Ulrike Mayer ◽  
Ulrike Hiller ◽  
Gerd Jürgens
Keyword(s):  
Cell Division ◽  
Membrane Vesicles ◽  
Time Frame ◽  
Snare Proteins ◽  
Long Distance ◽  
Directional Growth ◽  
Division Plane ◽  
Plant Cytokinesis ◽  
Plant Cell Division ◽  
Sites Of Action

Intracellular membrane fusion mediates diverse processes including cell growth, division and communication. Fusion involves complex formation between SNARE proteins anchored to adjacent membranes. How and in what form interacting SNARE proteins reach their sites of action is virtually unknown. We have addressed this problem in the context of plant cell division in which a large number of TGN-derived membrane vesicles fuse with one another to form the partitioning membrane. Blocking vesicle formation at the TGN revealed cis-SNARE complexes. These inactive cytokinetic SNARE complexes were already assembled at the endoplasmic reticulum and, after passage through Golgi/TGN to the cell division plane, transformed into fusogenic SNARE complexes. This mode of trafficking might ensure delivery of large stoichiometric quantities of SNARE proteins required for forming the partitioning membrane in the narrow time frame of plant cytokinesis. Such long-distance trafficking of inactive SNARE complexes would also facilitate directional growth processes during cell differentiation.

The role of the cytoskeleton and associated proteins in determination of the plant cell division plane

2013 ◽  
Vol 75 (2) ◽  
pp. 258-269 ◽  
Author(s):  
Carolyn G. Rasmussen ◽  
Amanda J. Wright ◽  
Sabine Müller
Keyword(s):  
Cell Division ◽  
Plant Cell ◽  
Division Plane ◽  
Plant Cell Division ◽  
Associated Proteins ◽  
Cell Division Plane

scholarly journals Functional characterization of the KNOLLE-interacting t-SNARE AtSNAP33 and its role in plant cytokinesis

2001 ◽  
Vol 155 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Maren Heese ◽  
Xavier Gansel ◽  
Liliane Sticher ◽  
Peter Wick ◽  
Markus Grebe ◽  
...  
Keyword(s):  
Cell Division ◽  
Membrane Fusion ◽  
Functional Characterization ◽  
Cell Plate ◽  
Yeast Two Hybrid ◽  
Division Plane ◽  
Plant Cytokinesis ◽  
Cell Plate Formation ◽  
Plate Formation ◽  
Two Hybrid

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.

scholarly journals Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Sandra Richter ◽  
Marika Kientz ◽  
Sabine Brumm ◽  
Mads Eggert Nielsen ◽  
Misoon Park ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Membrane Trafficking ◽  
Nucleotide Exchange ◽  
Division Plane ◽  
Plant Cytokinesis ◽  
Guanine Nucleotide Exchange ◽  
Cargo Delivery ◽  
Golgi Network ◽  
Cell Division Plane

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.

scholarly journals Functional analysis of the chromosomal passenger complex in Arabidopsis

2020 ◽  
Author(s):  
Shinichiro Komaki ◽  
Hidenori Takeuchi ◽  
Yuki Hamamura ◽  
Maren Heese ◽  
Takashi Hashimoto ◽  
...  
Keyword(s):  
Cell Division ◽  
Aurora B ◽  
Division Plane ◽  
Chromosomal Passenger ◽  
Full Complement ◽  
The One ◽  
Sites Of Action ◽  
Chromosome Passenger Complex ◽  
Mitosis And Meiosis ◽  
Kinetochore Function

SUMMARYA key regulator of cell division in all eukaryotes is the kinase Aurora B, which is encoded by the Aurora 3 (AUR3) gene in Arabidopsis. Aurora B has at least two central functions during cell division. On the one hand, it is essential for the correct, i.e. balanced, segregation of chromosomes in mitosis and meiosis by controlling kinetochore function. On the other hand, Aurora B acts at the division plane, where it is necessary to complete cytokinesis. To accomplish these two spatially distinct functions, Aurora B in animals is guided to its sites of action by Borealin, INCENP, and Survivin that build together with Aurora B the chromosome passenger complex (CPC). However, besides Aurora homologs, only a candidate gene with restricted homology to INCENP has so far been described in Arabidopsis raising the question whether there exists a full complement of the CPC in plants and how Aurora homologs are targeted subcellularly. Here, we have identified and functionally characterized a Borealin homolog, BOREALIN RELATED (BORR), in Arabidopsis. This, together with detailed localization studies including the putative Arabidopsis INCENP homolog, supports the existence of a CPC in plants.

scholarly journals Cell cortex microtubules contribute to division plane positioning during telophase in maize

2021 ◽  
Author(s):  
Marschal A. Bellinger ◽  
Aimee N. Uyehara ◽  
Pablo Martinez ◽  
Michael C. McCarthy ◽  
Carolyn G. Rasmussen
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
Cell Cortex ◽  
Cell Wall Formation ◽  
Division Plane ◽  
Specific Location ◽  
Division Site ◽  
Plant Cell Division ◽  
Defective Mutant ◽  
Transient Interactions

AbstractThe phragmoplast is a plant-specific microtubule and microfilament structure that forms during telophase to direct new cell wall formation. The phragmoplast expands towards a specific location at the cell cortex called the division site. How the phragmoplast accurately reaches the division site is currently unknown. We show that a previously uncharacterized microtubule arrays accumulated at the cell cortex. These microtubules were organized by transient interactions with division-site localized proteins and were then incorporated into the phragmoplast to guide it towards the division site. A phragmoplast-guidance defective mutant, tangled1, had aberrant cortical-telophase microtubule accumulation that correlated with phragmoplast positioning defects. Division-site localized proteins may promote proper division plane positioning by organizing the cortical-telophase microtubule array to guide the phragmoplast to the division site during plant cell division.One Sentence SummaryMicrotubules accumulate at the cell cortex and interact with the plant division machinery to direct its movement towards the division site.

Plant cytokinesis: a tale of membrane traffic and fusion

2015 ◽  
Vol 43 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Gerd Jürgens ◽  
Misoon Park ◽  
Sandra Richter ◽  
Sonja Touihri ◽  
Cornelia Krause ◽  
...  
Keyword(s):  
Higher Plants ◽  
Membrane Vesicles ◽  
Cell Plate ◽  
Division Plane ◽  
Daughter Cells ◽  
Division Site ◽  
Plant Cytokinesis ◽  
M Phase ◽  
Golgi Network ◽  
Sm Protein

Cytokinesis separates the forming daughter cells. Higher plants have lost the ability to constrict the plasma membrane (PM) in the division plane. Instead, trans-Golgi network (TGN)-derived membrane vesicles are targeted to the centre of the division plane and generate, by homotypic fusion, the partitioning membrane named cell plate (CP). The CP expands in a centrifugal fashion until its margin fuses with the PM at the cortical division site. Mutant screens in Arabidopsis have identified a cytokinesis-specific syntaxin named KNOLLE and an interacting Sec1/Munc18 (SM) protein named KEULE both of which are required for vesicle fusion during cytokinesis. KNOLLE is only made during M-phase, targeted to the division plane and degraded in the vacuole at the end of cytokinesis. Here we address mechanisms of KNOLLE trafficking and interaction of KNOLLE with different soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor (SNARE) partners and with SM-protein KEULE, ensuring membrane fusion in cytokinesis.

scholarly journals SepF is the FtsZ anchor in archaea, with features of an ancestral cell division system

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Nika Pende ◽  
Adrià Sogues ◽  
Daniela Megrian ◽  
Anna Sartori-Rupp ◽  
Patrick England ◽  
...  
Keyword(s):  
Cell Division ◽  
Common Ancestor ◽  
Phylogenetic Analyses ◽  
Super Resolution ◽  
Binding Mode ◽  
Last Universal Common Ancestor ◽  
Division Plane ◽  
Multiple Factors ◽  
Universal Common Ancestor ◽  
Super Resolution Microscopy

AbstractMost archaea divide by binary fission using an FtsZ-based system similar to that of bacteria, but they lack many of the divisome components described in model bacterial organisms. Notably, among the multiple factors that tether FtsZ to the membrane during bacterial cell constriction, archaea only possess SepF-like homologs. Here, we combine structural, cellular, and evolutionary analyses to demonstrate that SepF is the FtsZ anchor in the human-associated archaeon Methanobrevibacter smithii. 3D super-resolution microscopy and quantitative analysis of immunolabeled cells show that SepF transiently co-localizes with FtsZ at the septum and possibly primes the future division plane. M. smithii SepF binds to membranes and to FtsZ, inducing filament bundling. High-resolution crystal structures of archaeal SepF alone and in complex with the FtsZ C-terminal domain (FtsZCTD) reveal that SepF forms a dimer with a homodimerization interface driving a binding mode that is different from that previously reported in bacteria. Phylogenetic analyses of SepF and FtsZ from bacteria and archaea indicate that the two proteins may date back to the Last Universal Common Ancestor (LUCA), and we speculate that the archaeal mode of SepF/FtsZ interaction might reflect an ancestral feature. Our results provide insights into the mechanisms of archaeal cell division and pave the way for a better understanding of the processes underlying the divide between the two prokaryotic domains.

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