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Träfflista för sökning "WFRF:(Alvarado Kristensson Maria) srt2:(2020-2023)"

Search: WFRF:(Alvarado Kristensson Maria) > (2020-2023)

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1.
  • Alvarado Kristensson, Maria (author)
  • Choreography of the centrosome
  • 2020
  • In: Heliyon. - : Elsevier BV. - 2405-8440. ; 6:e03228, s. 1-6
  • Research review (peer-reviewed)abstract
    • More than a century ago, the centrosome was discovered and described as “the true division organ of the cell”. Electron microscopy revealed that a centrosome is an amorphous structure or pericentriolar protein matrix that surrounds a pair of well-organized centrioles. Today, the importance of the centrosome as a microtubule-organizing center and coordinator of the mitotic spindle is questioned, because centrioles are absent in up to half of all known eukaryotic species, and various mechanisms for acentrosomal microtubule nucleation have been described. This review recapitulates the known functions of centrosome movements in cellular homeostasis and discusses knowledge gaps in this field.
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2.
  • Alvarado Kristensson, Maria (author)
  • The Game of Tubulins
  • 2021
  • In: Cells. - : MDPI AG. - 2073-4409. ; 10
  • Research review (peer-reviewed)abstract
    • Members of the tubulin superfamily are GTPases; the activities of GTPases are necessary for life. The members of the tubulin superfamily are the constituents of the microtubules and the γ-tubulin meshwork. Mutations in members of the tubulin superfamily are involved in developmental brain disorders, and tubulin activities are the target for various chemotherapies. The intricate functions (game) of tubulins depend on the activities of the GTP-binding domain of α-, β-, and γ-tubulin. This review compares the GTP-binding domains of γ-tubulin, α-tubulin, and β-tubulin and, based on their similarities, recapitulates the known functions and the impact of the γ-tubulin GTP-binding domain in the regulation of the γ-tubulin meshwork and cellular homeostasis.
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3.
  • Corvaisier, Matthieu, et al. (author)
  • Non-Canonical Functions of the Gamma-Tubulin Meshwork in the Regulation of the Nuclear Architecture
  • 2020
  • In: Cancers. - : MDPI AG. - 2072-6694. ; 12:11
  • Research review (peer-reviewed)abstract
    • The nuclear architecture describes the organization of the various compartments in the nucleus of eukaryotic cells, where a plethora of processes such as nucleocytoplasmic transport, gene expression, and assembly of ribosomal subunits occur in a dynamic manner. During the different phases of the cell cycle, in post-mitotic cells and after oncogenic transformation, rearrangements of the nuclear architecture take place, and, among other things, these alterations result in reorganization of the chromatin and changes in gene expression. A member of the tubulin family, γtubulin, was first identified as part of a multiprotein complex that allows nucleation of microtubules. However, more than a decade ago, γtubulin was also characterized as a nuclear protein that modulates several crucial processes that affect the architecture of the nucleus. This review presents the latest knowledge regarding changes that arise in the nuclear architecture of healthy cells and under pathological conditions and, more specifically, considers the particular involvement of γtubulin in the modulation of the biology of the nuclear compartment.
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4.
  • Corvaisier, Matthieu, et al. (author)
  • The γ-tubulin meshwork assists in the recruitment of PCNA to chromatin in mammalian cells
  • 2021
  • In: Communications biology. - : Springer Science and Business Media LLC. - 2399-3642. ; 4:1, s. 767-
  • Journal article (peer-reviewed)abstract
    • Changes in the location of γ-tubulin ensure cell survival and preserve genome integrity. We investigated whether the nuclear accumulation of γ-tubulin facilitates the transport of proliferating cell nuclear antigen (PCNA) between the cytosolic and the nuclear compartment in mammalian cells. We found that the γ-tubulin meshwork assists in the recruitment of PCNA to chromatin. Also, decreased levels of γ-tubulin reduce the nuclear pool of PCNA. In addition, the γ-tubulin C terminus encodes a PCNA-interacting peptide (PIP) motif, and a γ-tubulin–PIP-mutant affects the nuclear accumulation of PCNA. In a cell-free system, PCNA and γ-tubulin formed a complex. In tumors, there is a significant positive correlation between TUBG1 and PCNA expression. Thus, we report a novel mechanism that constitutes the basis for tumor growth by which the γ-tubulin meshwork maintains indefinite proliferation by acting as an opportune scaffold for the transport of PCNA from the cytosol to the chromatin.
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5.
  • Malycheva, Darina, et al. (author)
  • Centrosome Movements Are TUBG1-Dependent
  • 2023
  • In: International Journal of Molecular Sciences. - 1422-0067. ; 24:17, s. 1-11
  • Journal article (peer-reviewed)abstract
    • The centrosome of mammalian cells is in constant movement and its motion plays a part in cell differentiation and cell division. The purpose of this study was to establish the involvement of the TUBG meshwork in centrosomal motility. In live cells, we used a monomeric red-fluorescenceprotein-tagged centrin 2 gene and a green-fluorescence-protein-tagged TUBG1 gene for labeling the centrosome and the TUBG1 meshwork, respectively. We found that centrosome movements occurredin cellular sites rich in GTPase TUBG1 and single-guide RNA mediated a reduction in the expression of TUBG1, altering the motility pattern of centrosomes. We propose that the TUBG1 meshwork enables the centrosomes to move by providing them with an interacting platform that mediates positional changes. These findings uncover a novel regulatory mechanism that controls the behavior of centrosomes.
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6.
  • Zhou, Jingkai, et al. (author)
  • Hubbing the cancer cell
  • 2022
  • In: Cancers. - : MDPI AG. - 2072-6694. ; 14:23
  • Research review (peer-reviewed)abstract
    • Simple SummaryCancer originates from changes in the genetics of single cells that affect their proliferative rate. To cope with the increased demand of building blocks and energy, tumor cells undergo adaptive changes creating new cellular homeostasis. These newly acquired traits are used clinically as diagnostic markers. Here, we summarize our knowledge of how a cell can adjust to new energetic demands during the transformation into a tumor cell.AbstractOncogenic transformation drives adaptive changes in a growing tumor that affect the cellular organization of cancerous cells, resulting in the loss of specialized cellular functions in the polarized compartmentalization of cells. The resulting altered metabolic and morphological patterns are used clinically as diagnostic markers. This review recapitulates the known functions of actin, microtubules and the γ-tubulin meshwork in orchestrating cell metabolism and functional cellular asymmetry.
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7.
  • Zhou, Jingkai, et al. (author)
  • Optimization of production of recombinant gamma-tubulin in bacteria
  • 2021
  • In: MethodsX. - : Elsevier BV. - 2215-0161. ; 8, s. 1-8
  • Journal article (peer-reviewed)abstract
    • Production of a protein of interest in bacteria and its purification from bacterial lysates are valuable tools for the purification of larger amounts of recombinant proteins. The low cost of culturing, and the rapid cell growth of bacteria make this host a good choice for protein production, but the folding and function of the purified protein might be altered due to the production of a eukaryotic protein in a prokaryotic host. Here, we provide a purification method for the purification of gamma (γ)-tubulin (TUBG) from soluble fractions of Escherichia (E.) coli lysates using affinity tags. This protocol describes a method that purifies soluble GST-TUBG1 from bacteria.  Of the three tested induction conditions, the highest yield of recombinant GST-TUBG1 was obtained after the induction of E. coli with isopropyl-D-1-thiogalactopyranoside (IPTG) for 1 h at 37°C followed by overnight incubation at room temperature. In comparison with other methodologies [1], the technique described here retrieves larger amounts of recombinant γ-tubulin from small-scale expression cultures.
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  • Result 1-7 of 7

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