The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation

2007 ◽  
Vol 21 (11) ◽  
pp. 2787-2797 ◽  
Author(s):  
Beatrice Chambraud ◽  
Hamida Belabes ◽  
Virginie Fontaine‐Lenoir ◽  
Arlette Fellous ◽  
Etienne Emile Baulieu
Keyword(s):  
Microtubule Formation

The in vitro effect of some nitroimidazoles on microtubule formation

1984 ◽  
Vol 33 (12) ◽  
pp. 1937-1940 ◽  
Author(s):  
M. Bendahmane ◽  
A.M. Chauvet Monges ◽  
D. Braguer ◽  
V. Peyrot ◽  
A. Crevat
Keyword(s):  
Microtubule Formation ◽  
Vitro Effect

scholarly journals Altered toxicity of the prion protein peptide PrP106–126 carrying the Ala117→Val mutation

2000 ◽  
Vol 346 (3) ◽  
pp. 785-791 ◽  
Author(s):  
David R. BROWN
Keyword(s):  
Point Mutation ◽  
Prion Protein ◽  
Prion Diseases ◽  
Point Mutations ◽  
Human Sequence ◽  
Gene Coding ◽  
Normal Human ◽  
Microtubule Formation ◽  
Β Sheet ◽  
Prion Protein Peptide

The inherited prion diseases such as Gerstmann-Sträussler-Scheinker syndrome (GSS) are linked to point mutations in the gene coding for the cellular isoform of the prion protein (PrPC). One particular point mutation A117V (Ala117 → Val) is linked to a variable pathology that usually includes deposition of neurofibrillary tangles. A prion protein peptide carrying this point mutation [PrP106-126(117V)] was generated and compared with a peptide based on the normal human sequence [PrP106-126(117A)]. The inclusion of this point mutation increased the toxicity of PrP106-126 which could be linked to an increased β-sheet content. An assay of microtubule formation in the presence of tau indicated that PrP106-126 decreased the rate of microtubule formation that could be related to the displacement of tau. PrP106-126 carrying the 117 mutation was more efficient at inhibiting microtubule formation. These results suggest a possible mechanism of toxicity for protein carrying this mutation via destabilization of the cytoskeleton and deposition of tau in filaments, as observed in GSS.

Mycotoxin Citrinin Induced Cell Cycle G2/M Arrest and Numerical Chromosomal Aberration Associated with Disruption of Microtubule Formation in Human Cells

2010 ◽  
Vol 119 (1) ◽  
pp. 84-92 ◽  
Author(s):  
Chia-Hao Chang ◽  
Feng-Yih Yu ◽  
Ting-Shun Wu ◽  
Li-Ting Wang ◽  
Biing-Hui Liu
Keyword(s):  
Cell Cycle ◽  
Chromosomal Aberration ◽  
Human Cells ◽  
Microtubule Formation

scholarly journals Modulation of microtubule dynamics by a TIR domain protein from the intracellular pathogen Brucella melitensis

2011 ◽  
Vol 439 (1) ◽  
pp. 79-83 ◽  
Author(s):  
Girish K. Radhakrishnan ◽  
Jerome S. Harms ◽  
Gary A. Splitter
Keyword(s):  
Brucella Melitensis ◽  
Interleukin 1 ◽  
Nuclear Factor Κb ◽  
Microtubule Dynamics ◽  
Innate Immune Responses ◽  
Tir Domain ◽  
Microtubule Stabilization ◽  
Loop Region ◽  
Microtubule Formation ◽  
Domain Protein

TIR (Toll/interleukin-1 receptor) domain-containing proteins play a crucial role in innate immunity in eukaryotes. Brucella is a highly infectious intracellular bacterium that encodes a TIR domain protein (TcpB) to subvert host innate immune responses to establish a beneficial niche for pathogenesis. TcpB inhibits NF-κB (nuclear factor κB) activation and pro-inflammatory cytokine secretions mediated by TLR (Toll-like receptor) 2 and TLR4. In the present study, we have demonstrated that TcpB modulates microtubule dynamics by acting as a stabilization factor. TcpB increased the rate of nucleation as well as the polymerization phases of microtubule formation in a similar manner to paclitaxel. TcpB could efficiently inhibit nocodazole- or cold-induced microtubule disassembly. Microtubule stabilization by TcpB is attributed to the BB-loop region of the TIR domain, and a point mutation affected the microtubule stabilization as well as the TLR-suppression properties of TcpB.

scholarly journals Distinct roles for antiparallel microtubule pairing and overlap during early spindle assembly

2013 ◽  
Vol 24 (20) ◽  
pp. 3238-3250 ◽  
Author(s):  
Elena Nazarova ◽  
Eileen O'Toole ◽  
Susi Kaitna ◽  
Paul Francois ◽  
Mark Winey ◽  
...  
Keyword(s):  
Electron Tomography ◽  
Dynamical Behavior ◽  
Three Dimensional ◽  
Spindle Assembly ◽  
Intermediate Step ◽  
High Angle ◽  
Normal Number ◽  
Spindle Poles ◽  
Evolutionarily Conserved ◽  
Microtubule Formation

During spindle assembly, microtubules may attach to kinetochores or pair to form antiparallel pairs or interpolar microtubules, which span the two spindle poles and contribute to mitotic pole separation and chromosome segregation. Events in the specification of the interpolar microtubules are poorly understood. Using three-dimensional electron tomography and analysis of spindle dynamical behavior in living cells, we investigated the process of spindle assembly. Unexpectedly, we found that the phosphorylation state of an evolutionarily conserved Cdk1 site (S360) in γ-tubulin is correlated with the number and organization of interpolar microtubules. Mimicking S360 phosphorylation (S360D) results in bipolar spindles with a normal number of microtubules but lacking interpolar microtubules. Inhibiting S360 phosphorylation (S360A) results in spindles with interpolar microtubules and high-angle, antiparallel microtubule pairs. The latter are also detected in wild-type spindles <1 μm in length, suggesting that high-angle microtubule pairing represents an intermediate step in interpolar microtubule formation. Correlation of spindle architecture with dynamical behavior suggests that microtubule pairing is sufficient to separate the spindle poles, whereas interpolar microtubules maintain the velocity of pole displacement during early spindle assembly. Our findings suggest that the number of interpolar microtubules formed during spindle assembly is controlled in part through activities at the spindle poles.

scholarly journals Identification and characterization of microtubule proteins from myxamoebae of Physarum polycephalum

1980 ◽  
Vol 189 (2) ◽  
pp. 305-312 ◽  
Author(s):  
A Roobol ◽  
C I Pogson ◽  
K Gull
Keyword(s):  
Physarum Polycephalum ◽  
Microtubule Assembly ◽  
Alpha Tubulin ◽  
Microtubule Associated Proteins ◽  
Cell Extracts ◽  
Microtubule Protein ◽  
Associated Proteins ◽  
Microtubule Formation

Cell extracts of myxamoebae of Physarum polycephalum have been prepared in such a way that they do not inhibit assembly of brain microtubule protein in vitro even at high extract-protein concentration. Co-polymers of these extracts and brain tubulin have been purified to constant stoichiometry and amoebal components identified by radiolabelling. Amoebal tubulin has been identified as having an alpha-subunit, mol.wt. 54 000, which co-migrates with brain alpha-tubulin and a beta-subunit, mol.wt. 50 000, which co-migrates with Tetrahymena ciliary beta-tubulin. Non-tubulin amoebal proteins that co-purify with tubulin during co-polymer formation have been shown to be essential for microtubule formation in the absence of glycerol and appear to be rather more effective than brain microtubule-associated proteins in stimulating assembly. The mitotic inhibitor griseofulvin (7-chloro-2′,4,6-trimethoxy-6′-methylspiro[benzofuran-2(3H),1′-cyclohex-2′-ene] −3,4′-dione), which binds to brain microtubule-associated proteins and inhibits brain microtubule assembly in vitro, affected co-polymer microtubule protein in a similar way, but to a slightly greater extent.

Cep120 promotes microtubule formation through a unique tubulin binding C2 domain

2018 ◽  
Vol 203 (1) ◽  
pp. 62-70 ◽  
Author(s):  
Ashwani Sharma ◽  
Samuel F. Gerard ◽  
Natacha Olieric ◽  
Michel O. Steinmetz
Keyword(s):  
C2 Domain ◽  
Tubulin Binding ◽  
Microtubule Formation

scholarly journals Eosinophil cytolysis on Immunoglobulin G is associated with microtubule formation and suppression of rho‐associated protein kinase signalling

2019 ◽  
Vol 50 (2) ◽  
pp. 198-212 ◽  
Author(s):  
Stephane Esnault ◽  
Jonathan P. Leet ◽  
Mats W. Johansson ◽  
Karina T. Barretto ◽  
Paul S. Fichtinger ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Immunoglobulin G ◽  
Microtubule Formation ◽  
Protein Kinase Signalling
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