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  1. Article ; Online: Anna Akhmanova: great tips on microtubules by Sedwick Caitlin.

    Akhmanova, Anna

    The Journal of cell biology

    2011  Volume 195, Issue 2, Page(s) 168–169

    MeSH term(s) History, 20th Century ; History, 21st Century ; Humans ; Microtubules ; Netherlands ; Research
    Language English
    Publishing date 2011-10-17
    Publishing country United States
    Document type Biography ; Historical Article ; Interview
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.1952pi
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  2. Article: Facilitating identification of minimal protein binding domains by cross-linking mass spectrometry

    Akhmanova, Anna

    Scientific reports, 7:13453

    2017  

    Abstract: Characterization of protein interaction domains is crucial for understanding protein functions. Here we combine cross-linking mass spectrometry (XL-MS) with deletion analysis to accurately locate minimal protein interaction domains. As a proof of concept, ...

    Institution Leibniz-Forschungsinstitut für Molekulare Pharmakologie
    Abstract Characterization of protein interaction domains is crucial for understanding protein functions. Here we combine cross-linking mass spectrometry (XL-MS) with deletion analysis to accurately locate minimal protein interaction domains. As a proof of concept, we investigated in detail the binding interfaces of two protein assemblies: the complex formed by MICAL3, ELKS and Rab8A, which is involved in exocytosis, and the complex of SLAIN2, CLASP2 and ch-TOG, which controls microtubule dynamics. We found that XL-MS provides valuable information to efficiently guide the design of protein fragments that are essential for protein interaction. However, we also observed a number of cross-links between polypeptide regions that were dispensable for complex formation, especially among intrinsically disordered sequences. Collectively, our results indicate that XL-MS, which renders distance restrains of linked residue pairs, accelerates the characterization of protein binding regions in combination with other biochemical approaches.
    Keywords Membrane trafficking ; Proteins
    Language English
    Document type Article
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  3. Article ; Online: Phase separation on microtubules: from droplet formation to cellular function?

    Volkov, Vladimir A / Akhmanova, Anna

    Trends in cell biology

    2023  Volume 34, Issue 1, Page(s) 18–30

    Abstract: Microtubules are cytoskeletal polymers that play important roles in numerous cellular processes, ranging from the control of cell shape and polarity to cell division and intracellular transport. Many of these roles rely on proteins that bind to ... ...

    Abstract Microtubules are cytoskeletal polymers that play important roles in numerous cellular processes, ranging from the control of cell shape and polarity to cell division and intracellular transport. Many of these roles rely on proteins that bind to microtubule ends and shafts, carry intrinsically disordered regions, and form complex multivalent interaction networks. A flurry of recent studies demonstrated that these properties allow diverse microtubule-binding proteins to undergo liquid-liquid phase separation (LLPS) in vitro. It is proposed that LLPS could potentially affect multiple microtubule-related processes, such as microtubule nucleation, control of microtubule dynamics and organization, and microtubule-based transport. Here, we discuss the evidence in favor and against the occurrence of LLPS and its functional significance for microtubule-based processes in cells.
    MeSH term(s) Humans ; Phase Separation ; Microtubules/metabolism ; Cytoskeleton/metabolism ; Protein Binding
    Language English
    Publishing date 2023-07-13
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2023.06.004
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  4. Article ; Online: Strengthening Microtubules by Cuts that Heal.

    Akhmanova, Anna

    Developmental cell

    2018  Volume 47, Issue 4, Page(s) 400–401

    Abstract: Microtubule-severing enzymes, which can remove tubulin dimers from microtubule lattices, participate in cytoskeletal remodeling in various contexts. A recent study showed that partially damaged microtubule shafts and new microtubule ends generated by ... ...

    Abstract Microtubule-severing enzymes, which can remove tubulin dimers from microtubule lattices, participate in cytoskeletal remodeling in various contexts. A recent study showed that partially damaged microtubule shafts and new microtubule ends generated by these enzymes can incorporate GTP-tubulin and serve as sites of microtubule rescue and re-growth, explaining how severing enzymes can amplify microtubule arrays.
    MeSH term(s) Cytoskeleton ; Guanosine Triphosphate ; Microtubules ; Tubulin
    Chemical Substances Tubulin ; Guanosine Triphosphate (86-01-1)
    Language English
    Publishing date 2018-11-10
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2018.11.002
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  5. Article ; Online: Mechanisms of microtubule organization in differentiated animal cells.

    Akhmanova, Anna / Kapitein, Lukas C

    Nature reviews. Molecular cell biology

    2022  Volume 23, Issue 8, Page(s) 541–558

    Abstract: Microtubules are polarized cytoskeletal filaments that serve as tracks for intracellular transport and form a scaffold that positions organelles and other cellular components and modulates cell shape and mechanics. In animal cells, the geometry, density ... ...

    Abstract Microtubules are polarized cytoskeletal filaments that serve as tracks for intracellular transport and form a scaffold that positions organelles and other cellular components and modulates cell shape and mechanics. In animal cells, the geometry, density and directionality of microtubule networks are major determinants of cellular architecture, polarity and proliferation. In dividing cells, microtubules form bipolar spindles that pull chromosomes apart, whereas in interphase cells, microtubules are organized in a cell type-specific fashion, which strongly correlates with cell physiology. In motile cells, such as fibroblasts and immune cells, microtubules are organized as radial asters, whereas in immotile epithelial and neuronal cells and in muscles, microtubules form parallel or antiparallel arrays and cortical meshworks. Here, we review recent work addressing how the formation of such microtubule networks is driven by the plethora of microtubule regulatory proteins. These include proteins that nucleate or anchor microtubule ends at different cellular structures and those that sever or move microtubules, as well as regulators of microtubule elongation, stability, bundling or modifications. The emerging picture, although still very incomplete, shows a remarkable diversity of cell-specific mechanisms that employ conserved building blocks to adjust microtubule organization in order to facilitate different cellular functions.
    MeSH term(s) Animals ; Biological Transport ; Cell Differentiation ; Cytoskeleton/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Organelles/metabolism
    Chemical Substances Microtubule-Associated Proteins
    Language English
    Publishing date 2022-04-05
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-022-00473-y
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  6. Article ; Online: Microtubules keep large cells in shape.

    Meiring, Joyce C M / Akhmanova, Anna

    The Journal of cell biology

    2020  Volume 219, Issue 6

    Abstract: Migrating cells need to coordinate extension and retraction of their protrusions to avoid fragmenting. Kopf et al. (2020. J. Cell Biol.https://doi.org/10.1083/jcb.201907154) demonstrate that microtubules help to maintain cell coherence during amoeboid ... ...

    Abstract Migrating cells need to coordinate extension and retraction of their protrusions to avoid fragmenting. Kopf et al. (2020. J. Cell Biol.https://doi.org/10.1083/jcb.201907154) demonstrate that microtubules help to maintain cell coherence during amoeboid migration by controlling actomyosin contractility in retracting protrusions.
    MeSH term(s) Actin Cytoskeleton ; Amoeba ; Cell Shape ; Microtubules
    Language English
    Publishing date 2020-05-07
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202004031
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  7. Article ; Online: Ten-fold Robust Expansion Microscopy.

    Damstra, Hugo G J / Mohar, Boaz / Eddison, Mark / Akhmanova, Anna / Kapitein, Lukas C / Tillberg, Paul W

    Bio-protocol

    2023  Volume 13, Issue 12, Page(s) e4698

    Abstract: Expansion microscopy (ExM) is a powerful technique to overcome the diffraction limit of light microscopy that can be applied in both tissues and cells. In ExM, samples are embedded in a swellable polymer gel to physically expand the sample and ... ...

    Abstract Expansion microscopy (ExM) is a powerful technique to overcome the diffraction limit of light microscopy that can be applied in both tissues and cells. In ExM, samples are embedded in a swellable polymer gel to physically expand the sample and isotropically increase resolution in x, y, and z. By systematic exploration of the ExM recipe space, we developed a novel ExM method termed Ten-fold Robust Expansion Microscopy (TREx) that, as the original ExM method, requires no specialized equipment or procedures. TREx enables ten-fold expansion of both thick mouse brain tissue sections and cultured human cells, can be handled easily, and enables high-resolution subcellular imaging with a single expansion step. Furthermore, TREx can provide ultrastructural context to subcellular protein localization by combining antibody-stained samples with off-the-shelf small molecule stains for both total protein and membranes.
    Language English
    Publishing date 2023-06-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2833269-6
    ISSN 2331-8325 ; 2331-8325
    ISSN (online) 2331-8325
    ISSN 2331-8325
    DOI 10.21769/BioProtoc.4698
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  8. Article ; Online: Microtubule minus-end regulation at a glance.

    Akhmanova, Anna / Steinmetz, Michel O

    Journal of cell science

    2019  Volume 132, Issue 11

    Abstract: Microtubules are cytoskeletal filaments essential for numerous aspects of cell physiology. They are polarized polymeric tubes with a fast growing plus end and a slow growing minus end. In this Cell Science at a Glance article and the accompanying poster, ...

    Abstract Microtubules are cytoskeletal filaments essential for numerous aspects of cell physiology. They are polarized polymeric tubes with a fast growing plus end and a slow growing minus end. In this Cell Science at a Glance article and the accompanying poster, we review the current knowledge on the dynamics and organization of microtubule minus ends. Several factors, including the γ-tubulin ring complex, CAMSAP/Patronin, ASPM/Asp, SPIRAL2 (in plants) and the KANSL complex recognize microtubule minus ends and regulate their nucleation, stability and interactions with partners, such as microtubule severing enzymes, microtubule depolymerases and protein scaffolds. Together with minus-end-directed motors, these microtubule minus-end targeting proteins (-TIPs) also control the formation of microtubule-organizing centers, such as centrosomes and spindle poles, and mediate microtubule attachment to cellular membrane structures, including the cell cortex, Golgi complex and the cell nucleus. Structural and functional studies are starting to reveal the molecular mechanisms by which dynamic -TIP networks control microtubule minus ends.
    MeSH term(s) Animals ; Cell Nucleus/metabolism ; Centrosome/metabolism ; Golgi Apparatus/metabolism ; Humans ; Microtubule-Associated Proteins/metabolism ; Microtubule-Organizing Center/metabolism ; Microtubules/metabolism ; Spindle Poles/metabolism
    Chemical Substances Microtubule-Associated Proteins
    Language English
    Publishing date 2019-06-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.227850
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  9. Article ; Online: Correction: Visualizing cellular and tissue ultrastructure using Ten-fold Robust Expansion Microscopy (TREx).

    Damstra, Hugo G J / Mohar, Boaz / Eddison, Mark / Akhmanova, Anna / Kapitein, Lukas C / Tillberg, Paul W

    eLife

    2022  Volume 11

    Language English
    Publishing date 2022-11-29
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.85169
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  10. Article ; Online: More is not always better: hyperglutamylation leads to neurodegeneration.

    Akhmanova, Anna / Hoogenraad, Casper C

    The EMBO journal

    2018  Volume 37, Issue 23

    MeSH term(s) Animals ; Humans ; Mice ; Microtubules/genetics ; Microtubules/metabolism ; Microtubules/pathology ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Peptides/genetics ; Peptides/metabolism ; Protein Processing, Post-Translational ; Tubulin/genetics ; Tubulin/metabolism
    Chemical Substances Peptides ; Tubulin ; polyglutamine (26700-71-0)
    Language English
    Publishing date 2018-11-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2018101023
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