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  1. Article ; Online: Linking cortical microtubule attachment and exocytosis [version 1; referees

    Ivar Noordstra / Anna Akhmanova

    F1000Research, Vol

    2 approved]

    2017  Volume 6

    Abstract: Exocytosis is a fundamental cellular process whereby secreted molecules are packaged into vesicles that move along cytoskeletal filaments and fuse with the plasma membrane. To function optimally, cells are strongly dependent on precisely controlled ... ...

    Abstract Exocytosis is a fundamental cellular process whereby secreted molecules are packaged into vesicles that move along cytoskeletal filaments and fuse with the plasma membrane. To function optimally, cells are strongly dependent on precisely controlled delivery of exocytotic cargo. In mammalian cells, microtubules serve as major tracks for vesicle transport by motor proteins, and thus microtubule organization is important for targeted delivery of secretory carriers. Over the years, multiple microtubule-associated and cortical proteins have been discovered that facilitate the interaction between the microtubule plus ends and the cell cortex. In this review, we focus on mammalian protein complexes that have been shown to participate in both cortical microtubule capture and exocytosis, thereby regulating the spatial organization of secretion. These complexes include microtubule plus-end tracking proteins, scaffolding factors, actin-binding proteins, and components of vesicle docking machinery, which together allow efficient coordination of cargo transport and release.
    Keywords Cell Adhesion ; Cell Growth & Division ; Cytoskeleton ; Membranes & Sorting ; Morphogenesis & Cell Biology ; Neuronal & Glial Cell Biology ; Neuronal Signaling Mechanisms ; Pattern Formation ; Medicine ; R ; Science ; Q
    Subject code 571 ; 612
    Language English
    Publishing date 2017-04-01T00:00:00Z
    Publisher F1000 Research Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Publishing in the time of COVID-19

    Michael B Eisen / Anna Akhmanova / Timothy E Behrens / Detlef Weigel

    eLife, Vol

    2020  Volume 9

    Abstract: eLife is making changes to its policies on peer review in response to the impact of COVID-19 on the scientific community. ...

    Abstract eLife is making changes to its policies on peer review in response to the impact of COVID-19 on the scientific community.
    Keywords scientific publishing ; peer review ; preprints ; early-career researchers ; COVID-19 ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-03-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Visualizing cellular and tissue ultrastructure using Ten-fold Robust Expansion Microscopy (TREx)

    Hugo GJ Damstra / Boaz Mohar / Mark Eddison / Anna Akhmanova / Lukas C Kapitein / Paul W Tillberg

    eLife, Vol

    2022  Volume 11

    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. The maximum resolution increase is limited by the expansion factor of the gel, which is four-fold for the original ExM protocol. Variations on the original ExM method have been reported that allow for greater expansion factors but at the cost of ease of adoption or versatility. Here, we systematically explore the ExM recipe space and present a novel method termed Ten-fold Robust Expansion Microscopy (TREx) that, like the original ExM method, requires no specialized equipment or procedures. We demonstrate that TREx gels expand 10-fold, can be handled easily, and can be applied to both thick mouse brain tissue sections and cultured human cells enabling high-resolution subcellular imaging with a single expansion step. Furthermore, we show that 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.
    Keywords super-resolution ; expansion microscopy ; sub-organelle imaging ; immunofluorescence ; light microscopy ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-02-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Correction

    Hugo GJ Damstra / Boaz Mohar / Mark Eddison / Anna Akhmanova / Lukas C Kapitein / Paul W Tillberg

    eLife, Vol

    Visualizing cellular and tissue ultrastructure using Ten-fold Robust Expansion Microscopy (TREx)

    2022  Volume 11

    Keywords Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-11-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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  5. Article ; Online: Rigorous review and editorial oversight of clinical preprints

    Mone Zaidi / Diane M Harper / Anna Akhmanova / Detlef Weigel / Timothy E Behrens / Michael B Eisen

    eLife, Vol

    2021  Volume 10

    Abstract: Research in many different areas of medicine will benefit from new approaches to peer review and publishing. ...

    Abstract Research in many different areas of medicine will benefit from new approaches to peer review and publishing.
    Keywords medicine ; public health ; physician-scientists ; peer review ; preprints ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-06-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Implementing a "publish, then review" model of publishing

    Michael B Eisen / Anna Akhmanova / Timothy E Behrens / Diane M Harper / Detlef Weigel / Mone Zaidi

    eLife, Vol

    2020  Volume 9

    Abstract: From July 2021 eLife will only review manuscripts already published as preprints, and will focus its editorial process on producing public reviews to be posted alongside the preprints. ...

    Abstract From July 2021 eLife will only review manuscripts already published as preprints, and will focus its editorial process on producing public reviews to be posted alongside the preprints.
    Keywords scientific publishing ; peer review ; preprints ; research communication ; research assessment ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-12-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Control of endothelial cell polarity and sprouting angiogenesis by non-centrosomal microtubules

    Maud Martin / Alexandra Veloso / Jingchao Wu / Eugene A Katrukha / Anna Akhmanova

    eLife, Vol

    2018  Volume 7

    Abstract: Microtubules control different aspects of cell polarization. In cells with a radial microtubule system, a pivotal role in setting up asymmetry is attributed to the relative positioning of the centrosome and the nucleus. Here, we show that centrosome loss ...

    Abstract Microtubules control different aspects of cell polarization. In cells with a radial microtubule system, a pivotal role in setting up asymmetry is attributed to the relative positioning of the centrosome and the nucleus. Here, we show that centrosome loss had no effect on the ability of endothelial cells to polarize and move in 2D and 3D environments. In contrast, non-centrosomal microtubules stabilized by the microtubule minus-end-binding protein CAMSAP2 were required for directional migration on 2D substrates and for the establishment of polarized cell morphology in soft 3D matrices. CAMSAP2 was also important for persistent endothelial cell sprouting during in vivo zebrafish vessel development. In the absence of CAMSAP2, cell polarization in 3D could be partly rescued by centrosome depletion, indicating that in these conditions the centrosome inhibited cell polarity. We propose that CAMSAP2-protected non-centrosomal microtubules are needed for establishing cell asymmetry by enabling microtubule enrichment in a single-cell protrusion.
    Keywords Centrosome ; cell migration ; microtubule ; CAMSAP ; Golgi apparatus ; endothelium ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2018-03-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: WDR47 protects neuronal microtubule minus ends from katanin-mediated severing

    Robin R. Buijs / Jessica J.A. Hummel / Mithila Burute / Xingxiu Pan / Yujie Cao / Riccardo Stucchi / Maarten Altelaar / Anna Akhmanova / Lukas C. Kapitein / Casper C. Hoogenraad

    Cell Reports, Vol 36, Iss 2, Pp 109371- (2021)

    2021  

    Abstract: Summary: Axons and dendrites are long extensions of neurons that contain arrays of noncentrosomal microtubules. Calmodulin-regulated spectrin-associated proteins (CAMSAPs) bind to and stabilize free microtubule minus ends and are critical for proper ... ...

    Abstract Summary: Axons and dendrites are long extensions of neurons that contain arrays of noncentrosomal microtubules. Calmodulin-regulated spectrin-associated proteins (CAMSAPs) bind to and stabilize free microtubule minus ends and are critical for proper neuronal development and function. Previous studies have shown that the microtubule-severing ATPase katanin interacts with CAMSAPs and limits the length of CAMSAP-decorated microtubule stretches. However, how CAMSAP and microtubule minus end dynamics are regulated in neurons is poorly understood. Here, we show that the neuron-enriched protein WDR47 interacts with CAMSAPs and is critical for axon and dendrite development. We find that WDR47 accumulates at CAMSAP2-decorated microtubules, is essential for maintaining CAMSAP2 stretches, and protects minus ends from katanin-mediated severing. We propose a model where WDR47 protects CAMSAP2 at microtubule minus ends from katanin activity to ensure proper stabilization of the neuronal microtubule network.
    Keywords neuron ; axon ; dendrite ; microtubule ; centrosome ; WDR47 ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2021-07-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Facilitating identification of minimal protein binding domains by cross-linking mass spectrometry

    Qingyang Liu / Sanne Remmelzwaal / Albert J. R. Heck / Anna Akhmanova / Fan Liu

    Scientific Reports, Vol 7, Iss 1, Pp 1-

    2017  Volume 11

    Abstract: 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 ... ...

    Abstract 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 Medicine ; R ; Science ; Q
    Language English
    Publishing date 2017-10-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Optogenetic dissection of mitotic spindle positioning in vivo

    Lars-Eric Fielmich / Ruben Schmidt / Daniel J Dickinson / Bob Goldstein / Anna Akhmanova / Sander van den Heuvel

    eLife, Vol

    2018  Volume 7

    Abstract: The position of the mitotic spindle determines the plane of cell cleavage, and thereby daughter cell location, size, and content. Spindle positioning is driven by dynein-mediated pulling forces exerted on astral microtubules, which requires an ... ...

    Abstract The position of the mitotic spindle determines the plane of cell cleavage, and thereby daughter cell location, size, and content. Spindle positioning is driven by dynein-mediated pulling forces exerted on astral microtubules, which requires an evolutionarily conserved complex of Gα∙GDP, GPR-1/2Pins/LGN, and LIN-5Mud/NuMA proteins. To examine individual functions of the complex components, we developed a genetic strategy for light-controlled localization of endogenous proteins in C. elegans embryos. By replacing Gα and GPR-1/2 with a light-inducible membrane anchor, we demonstrate that Gα∙GDP, Gα∙GTP, and GPR-1/2 are not required for pulling-force generation. In the absence of Gα and GPR-1/2, cortical recruitment of LIN-5, but not dynein itself, induced high pulling forces. The light-controlled localization of LIN-5 overruled normal cell-cycle and polarity regulation and provided experimental control over the spindle and cell-cleavage plane. Our results define Gα∙GDP–GPR-1/2Pins/LGN as a regulatable membrane anchor, and LIN-5Mud/NuMA as a potent activator of dynein-dependent spindle-positioning forces.
    Keywords optogenetics ; mitotic spindle positioning ; dynein ; germline silencing ; LIN-5 (NuMA) ; cell division ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2018-08-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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