ring assembly
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2022 ◽  
Author(s):  
Imge Ozugergin ◽  
Karina Mastronardi ◽  
Chris Law ◽  
Alisa Piekny

Cytokinesis occurs at the end of mitosis due to the ingression of a contractile ring that cleaves the daughter cells. The core machinery regulating this crucial process is conserved among metazoans. Multiple pathways control ring assembly, but their contribution in different cell types is not known. We found that in the C. elegans embryo, AB and P1 cells fated to be somatic tissue and germline, respectively, have different cytokinesis kinetics supported by distinct myosin levels and organization. Through perturbation of RhoA or polarity regulators and the generation of tetraploid strains, we found that ring assembly is controlled by multiple fate-dependent factors that include myosin-levels, and mechanisms that respond to cell size. Active Ran coordinates ring position with the segregating chromatids in HeLa cells by forming an inverse gradient with importins that control the cortical recruitment of anillin. We found that the Ran pathway regulates anillin in AB cells, but functions differently in P1 cells. We propose that ring assembly delays in P1 cells caused by low myosin and Ran signaling coordinate the timing of ring closure with their somatic neighbours.


2021 ◽  
Vol 2021 ◽  
pp. 1-14
Author(s):  
Guoping Zheng ◽  
Jurij Karlovsek

Universal tapered segmental ring system has been adopted to assemble tangent and curve line elements into the shield tunnels through the relative rotation of the adjacent front and rear rings, which simplifies the formwork design, demonstrates strong universality, and is easy for quality assurance. To evaluate the position deviation caused by the taper value and propose the assembly scheme for the contractor, this article developed the universal tapered segmental ring assembly simulation technology. Firstly, the assembly procedure of the universal tapered segmental ring system both in normal case and in special case is introduced, including the interval tunnel of special rings and actual engineering that needs deviation correction. Secondly, relevant core algorithms are introduced in detail, including the coordinate position algorithm of horizontal and vertical curves and computer graphic algorithm of spatial point rotating around any axis. Finally, this article takes a background metro line tunnel as a case to validate the algorithm and illustrate the assessment methodology of universal tapered segmental ring assembly accuracy. The sections with maximum deviation are found as an alert ahead of the shield advancing. In conclusion, the algorithms and methodology proposed in this article illustrate the excellent suitability and robustness in shield tunnels adopting a universal tapered segmental ring system in the stage of both design and construction.


2021 ◽  
Vol 2057 (1) ◽  
pp. 012038
Author(s):  
M V Alekseev ◽  
S I Lezhnin

Abstract Gas outflow into a cavity with different annular assembly filled with liquid by the VOF method, supplemented by the k-ε turbulence model, is numerically simulated. Calculations are performed for three types of ring assembly. Principal scenarios of bubble growth outside the assembly and annular jets inside it are obtained. The characteristic expiration times are investigated.


Cells ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2336
Author(s):  
Stefano Sechi ◽  
Angela Karimpour-Ghahnavieh ◽  
Anna Frappaolo ◽  
Laura Di Francesco ◽  
Roberto Piergentili ◽  
...  

Golgi phosphoprotein 3 (GOLPH3) is a highly conserved peripheral membrane protein localized to the Golgi apparatus and the cytosol. GOLPH3 binding to Golgi membranes depends on phosphatidylinositol 4-phosphate [PI(4)P] and regulates Golgi architecture and vesicle trafficking. GOLPH3 overexpression has been correlated with poor prognosis in several cancers, but the molecular mechanisms that link GOLPH3 to malignant transformation are poorly understood. We recently showed that PI(4)P-GOLPH3 couples membrane trafficking with contractile ring assembly during cytokinesis in dividing Drosophila spermatocytes. Here, we use affinity purification coupled with mass spectrometry (AP-MS) to identify the protein-protein interaction network (interactome) of Drosophila GOLPH3 in testes. Analysis of the GOLPH3 interactome revealed enrichment for proteins involved in vesicle-mediated trafficking, cell proliferation and cytoskeleton dynamics. In particular, we found that dGOLPH3 interacts with the Drosophila orthologs of Fragile X mental retardation protein and Ataxin-2, suggesting a potential role in the pathophysiology of disorders of the nervous system. Our findings suggest novel molecular targets associated with GOLPH3 that might be relevant for therapeutic intervention in cancers and other human diseases.


2021 ◽  
Author(s):  
Alexander Dudziak ◽  
Lena Engelhard ◽  
Cole Bourque ◽  
Björn Udo Klink ◽  
Pascaline Rombaut ◽  
...  
Keyword(s):  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Akihiro Kawamoto ◽  
Tomoko Miyata ◽  
Fumiaki Makino ◽  
Miki Kinoshita ◽  
Tohru Minamino ◽  
...  

AbstractThe bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. The C ring attached to the MS ring is involved in torque generation and rotation switch, and a large symmetry mismatch between these two rings has been a long puzzle, especially with respect to their role in motor function. Here, using cryoEM structural analysis of the flagellar basal body and the MS ring formed by full-length FliF from Salmonella enterica, we show that the native MS ring is formed by 34 FliF subunits with no symmetry variation. Symmetry analysis of the C ring shows a variation with a peak at 34-fold, suggesting flexibility in C ring assembly. Finally, our data also indicate that FliF subunits assume two different conformations, contributing differentially to the inner and middle parts of the M ring and thus resulting in 23- and 11-fold subsymmetries in the inner and middle M ring, respectively. The internal core of the M ring, formed by 23 subunits, forms a hole of the right size to accommodate the protein export gate.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Georgios N. Hatzopoulos ◽  
Tim Kükenshöner ◽  
Niccolò Banterle ◽  
Tatiana Favez ◽  
Isabelle Flückiger ◽  
...  

AbstractCentrioles are evolutionarily conserved multi-protein organelles essential for forming cilia and centrosomes. Centriole biogenesis begins with self-assembly of SAS-6 proteins into 9-fold symmetrical ring polymers, which then stack into a cartwheel that scaffolds organelle formation. The importance of this architecture has been difficult to decipher notably because of the lack of precise tools to modulate the underlying assembly reaction. Here, we developed monobodies against Chlamydomonas reinhardtii SAS-6, characterizing three in detail with X-ray crystallography, atomic force microscopy and cryo-electron microscopy. This revealed distinct monobody-target interaction modes, as well as specific consequences on ring assembly and stacking. Of particular interest, monobody MBCRS6-15 induces a conformational change in CrSAS-6, resulting in the formation of a helix instead of a ring. Furthermore, we show that this alteration impairs centriole biogenesis in human cells. Overall, our findings identify monobodies as powerful molecular levers to alter the architecture of multi-protein complexes and tune centriole assembly.


PLoS ONE ◽  
2021 ◽  
Vol 16 (6) ◽  
pp. e0252800
Author(s):  
Lucas Kuhlen ◽  
Steven Johnson ◽  
Jerry Cao ◽  
Justin C. Deme ◽  
Susan M. Lea

Type three secretion is the mechanism of protein secretion found in bacterial flagella and injectisomes. At its centre is the export apparatus (EA), a complex of five membrane proteins through which secretion substrates pass the inner membrane. While the complex formed by four of the EA proteins has been well characterised structurally, little is known about the structure of the membrane domain of the largest subunit, FlhA in flagella, SctV in injectisomes. Furthermore, the biologically relevant nonameric assembly of FlhA/SctV has been infrequently observed and differences in conformation of the cytoplasmic portion of FlhA/SctV between open and closed states have been suggested to reflect secretion system specific differences. FlhA has been shown to bind to chaperone-substrate complexes in an open state, but in previous assembled ring structures, SctV is in a closed state. Here, we identify FlhA and SctV homologues that can be recombinantly produced in the oligomeric state and study them using cryo-electron microscopy. The structures of the cytoplasmic domains from both FlhA and SctV are in the open state and we observe a conserved interaction between a short stretch of residues at the N-terminus of the cytoplasmic domain, known as FlhAL/SctVL, with a groove on the adjacent protomer’s cytoplasmic domain, which stabilises the nonameric ring assembly.


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