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  1. Article ; Online: Editorial overview: Functional specialization of the cytoskeleton in diverse cell types.

    Marston, Adele L / Tyska, Matthew J

    Current opinion in cell biology

    2024  Volume 87, Page(s) 102343

    MeSH term(s) Cytoskeleton/metabolism ; Microtubules
    Language English
    Publishing date 2024-02-23
    Publishing country England
    Document type Editorial
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2024.102343
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2963: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article: Mitotic spindle positioning protein (MISP) is an actin bundler that senses ADP-actin and binds near the pointed ends of filaments.

    Morales, E Angelo / Tyska, Matthew J

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Actin bundling proteins crosslink filaments into polarized structures that shape and support membrane protrusions including filopodia, microvilli, and stereocilia. In the case of epithelial microvilli, mitotic spindle positioning protein (MISP) is an ... ...

    Abstract Actin bundling proteins crosslink filaments into polarized structures that shape and support membrane protrusions including filopodia, microvilli, and stereocilia. In the case of epithelial microvilli, mitotic spindle positioning protein (MISP) is an actin bundler that localizes specifically to the basal rootlets, where the pointed ends of core bundle filaments converge. Previous studies established that MISP is prevented from binding more distal segments of the core bundle by competition with other actin binding proteins. Yet whether MISP holds a preference for binding directly to rootlet actin remains an open question. Using
    Language English
    Publishing date 2023-05-06
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.05.05.539649
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: BioID2 screening identifies KIAA1671 as an EPS8 proximal factor that marks sites of microvillus growth.

    Gaeta, Isabella M / Tyska, Matthew J

    Molecular biology of the cell

    2023  Volume 34, Issue 4, Page(s) ar31

    Abstract: Microvilli are defining morphological features of the apical surfaces in diverse epithelial tissues. To develop our understanding of microvillus biogenesis, we used a biotin proximity-labeling approach to uncover new molecules enriched near EPS8, a well- ... ...

    Abstract Microvilli are defining morphological features of the apical surfaces in diverse epithelial tissues. To develop our understanding of microvillus biogenesis, we used a biotin proximity-labeling approach to uncover new molecules enriched near EPS8, a well-studied marker of the microvillus distal tip compartment. Mass spectrometry of biotinylated hits identified KIAA1671, a large (∼200 kDa), disordered, and previously uncharacterized protein. Based on immunofluorescent staining and expression of fluorescent protein-tagged constructs, we found that KIAA1671 localizes to the base of the brush border in native intestinal tissue and polarized epithelial-cell culture models, as well as dynamic actin-rich structures in unpolarized, nonepithelial cell types. Live imaging also revealed that during the early stages of microvillar growth, KIAA1671 colocalizes with EPS8 in diffraction-limited puncta. However, once elongation of the core bundle begins, these two factors separate, with EPS8 tracking the distal end and KIAA1671 remaining behind at the base of the structure. These results suggest that KIAA1671 cooperates with EPS8 and potentially other assembly factors to initiate growth of microvilli on the apical surface. These findings offer new details on how transporting epithelial cells builds the brush border and may inform our understanding of how apical specializations are assembled in other epithelial contexts.
    MeSH term(s) Actins/metabolism ; Epithelial Cells/metabolism ; Microvilli/metabolism ; RNA-Binding Proteins/metabolism
    Chemical Substances Actins ; RNA-Binding Proteins
    Language English
    Publishing date 2023-02-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E22-11-0498
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Loss of intermicrovillar adhesion impairs basolateral junctional complexes in transporting epithelia.

    Cencer, Caroline S / Robinson, Kianna L / Tyska, Matthew J

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Transporting epithelial cells in the gut and kidney rely on protocadherin-based apical adhesion complexes to organize microvilli that extend into the luminal space. In these systems, CDHR2 and CDHR5 localize to the distal ends of microvilli, where they ... ...

    Abstract Transporting epithelial cells in the gut and kidney rely on protocadherin-based apical adhesion complexes to organize microvilli that extend into the luminal space. In these systems, CDHR2 and CDHR5 localize to the distal ends of microvilli, where they form an intermicrovillar adhesion complex (IMAC) that links the tips of these structures, promotes the formation of a well-ordered array of protrusions, and in turn maximizes apical membrane surface area. Recently, we discovered that IMACs can also form between microvilli that extend from neighboring cells, across cell-cell junctions. As an additional point of physical contact between cells, transjunctional IMACs are well positioned to impact the integrity of canonical tight and adherens junctions that form more basolaterally. Here, we sought to test this idea using cell culture and mouse models that lacked CDHR2 expression and were unable to form IMACs. CDHR2 knockout perturbed cell and junction morphology, led to loss of key components from tight and adherens junctions, and impaired barrier function and wound healing. These results indicate that, in addition to organizing apical microvilli, IMACs provide a layer of cell-cell contact that functions in parallel with canonical tight and adherens junctions to support the physiological functions of transporting epithelia.
    Language English
    Publishing date 2024-03-19
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.03.19.585733
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Mitotic spindle positioning protein (MISP) preferentially binds to aged F-actin.

    Morales, E Angelo / Fitz, Gillian N / Tyska, Matthew J

    The Journal of biological chemistry

    2024  , Page(s) 107279

    Abstract: Actin bundling proteins crosslink filaments into polarized structures that shape and support membrane protrusions including filopodia, microvilli, and stereocilia. In the case of epithelial microvilli, mitotic spindle positioning protein (MISP) is an ... ...

    Abstract Actin bundling proteins crosslink filaments into polarized structures that shape and support membrane protrusions including filopodia, microvilli, and stereocilia. In the case of epithelial microvilli, mitotic spindle positioning protein (MISP) is an actin bundler that localizes specifically to the basal rootlets, where the pointed ends of core bundle filaments converge. Previous studies established that MISP is prevented from binding more distal segments of the core bundle by competition with other actin binding proteins. Yet whether MISP holds a preference for binding directly to rootlet actin remains an open question. By immunostaining native intestinal tissue sections, we found that microvillar rootlets are decorated with the severing protein, cofilin, suggesting high levels of ADP-actin in these structures. Using TIRF microscopy assays, we also found that purified MISP exhibits a binding preference for ADP- vs. ADP-Pi-actin containing filaments. Consistent with this, assays with actively growing actin filaments revealed that MISP binds at or near their pointed ends. Moreover, although substrate attached MISP assembles filament bundles in parallel and antiparallel configurations, in solution MISP assembles parallel bundles consisting of multiple filaments exhibiting uniform polarity. These discoveries highlight nucleotide state sensing as a mechanism for sorting actin bundlers along filaments and driving their accumulation near filament ends. Such localized binding might drive parallel bundle formation and/or locally modulate bundle mechanical properties in microvilli and related protrusions.
    Language English
    Publishing date 2024-04-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2024.107279
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Building the brush border, one microvillus at a time.

    Morales, E Angelo / Gaeta, Isabella / Tyska, Matthew J

    Current opinion in cell biology

    2023  Volume 80, Page(s) 102153

    Abstract: Microvilli are actin bundle-supported surface protrusions assembled by diverse cell types to mediate biochemical and physical interactions with the external environment. Found on the surface of some of the earliest animal cells, primordial microvilli ... ...

    Abstract Microvilli are actin bundle-supported surface protrusions assembled by diverse cell types to mediate biochemical and physical interactions with the external environment. Found on the surface of some of the earliest animal cells, primordial microvilli likely contributed to bacterial entrapment and feeding. Although millions of years of evolution have repurposed these protrusions to fulfill diverse roles such as detection of mechanical or visual stimuli in inner ear hair cells or retinal pigmented epithelial cells, respectively, solute uptake remains a key essential function linked to these structures. In this mini review, we offer a brief overview of the composition and structure of epithelial microvilli, highlight recent discoveries on the growth of these protrusions early in differentiation, and point to fundamental questions surrounding microvilli biogenesis that remain open for future studies.
    MeSH term(s) Animals ; Microvilli/metabolism ; Actins/metabolism
    Chemical Substances Actins
    Language English
    Publishing date 2023-02-22
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2023.102153
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    ab Jg. 2022: Lesesaal (EG)

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  7. Article: Intestinal tuft cells assemble a cytoskeletal superstructure composed of co-aligned actin bundles and microtubules.

    Silverman, Jennifer B / Krystofiak, Evan E / Caplan, Leah R / Lau, Ken S / Tyska, Matthew J

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Background & aims: All tissues consist of a distinct set of cell types, which collectively support organ function and homeostasis. Tuft cells are a rare epithelial cell type found in diverse epithelia, where they play important roles in sensing antigens ...

    Abstract Background & aims: All tissues consist of a distinct set of cell types, which collectively support organ function and homeostasis. Tuft cells are a rare epithelial cell type found in diverse epithelia, where they play important roles in sensing antigens and stimulating downstream immune responses. Exhibiting a unique polarized morphology, tuft cells are defined by an array of giant actin filament bundles that support ∼2 μm of apical membrane protrusion and extend over 7 μm towards the cell's perinuclear region. Despite their established roles in maintaining intestinal epithelial homeostasis, tuft cells remain understudied due to their rarity (e.g. ∼ 1% in the small intestinal epithelium). Details regarding the ultrastructural organization of the tuft cell cytoskeleton, the molecular components involved in building the array of giant actin bundles, and how these cytoskeletal structures support tuft cell biology remain unclear.
    Methods: To begin to answer these questions, we used advanced light and electron microscopy to perform quantitative morphometry of the small intestinal tuft cell cytoskeleton.
    Results: We found that tuft cell core bundles consist of actin filaments that are crosslinked in a parallel "barbed-end out" configuration. These polarized structures are also supported by a unique group of tuft cell enriched actin-binding proteins that are differentially localized along the giant core bundles. Furthermore, we found that tuft cell actin bundles are co-aligned with a highly ordered network of microtubules.
    Conclusions: Tuft cells assemble a cytoskeletal superstructure that is well positioned to serve as a track for subcellular transport along the apical-basolateral axis and in turn, support the dynamic sensing functions that are critical for intestinal epithelial homeostasis.
    Synopsis: This research leveraged advanced light and electron microscopy to perform quantitative morphometry of the intestinal tuft cell cytoskeleton. Three-dimensional reconstructions of segmented image data revealed a co-aligned actin-microtubule superstructure that may play a fundamental role in tuft cell function.
    Language English
    Publishing date 2024-03-19
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.03.19.585757
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Nectin-3 and shed forms of CSPG4 can serve as epithelial cell receptors for

    Childress, Kevin O / Cencer, Caroline S / Tyska, Matthew J / Lacy, D Borden

    mBio

    2023  Volume 14, Issue 5, Page(s) e0185723

    Abstract: Importance: Toxin B (TcdB) is a major virulence factor ... ...

    Abstract Importance: Toxin B (TcdB) is a major virulence factor of
    MeSH term(s) Bacterial Toxins/metabolism ; Clostridioides difficile ; Nectins/metabolism ; Epithelial Cells/metabolism ; Receptors, Cell Surface/metabolism ; Bacterial Proteins/metabolism
    Chemical Substances Bacterial Toxins ; Nectins ; Receptors, Cell Surface ; Bacterial Proteins
    Language English
    Publishing date 2023-09-25
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.01857-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Intestinal Tuft Cells: Morphology, Function, and Implications for Human Health.

    Silverman, Jennifer B / Vega, Paige N / Tyska, Matthew J / Lau, Ken S

    Annual review of physiology

    2023  Volume 86, Page(s) 479–504

    Abstract: Tuft cells are a rare and morphologically distinct chemosensory cell type found throughout many organs, including the gastrointestinal tract. These cells were identified by their unique morphologies distinguished by large apical protrusions. ... ...

    Abstract Tuft cells are a rare and morphologically distinct chemosensory cell type found throughout many organs, including the gastrointestinal tract. These cells were identified by their unique morphologies distinguished by large apical protrusions. Ultrastructural data have begun to describe the molecular underpinnings of their cytoskeletal features, and tuft cell-enriched cytoskeletal proteins have been identified, although the connection of tuft cell morphology to tuft cell functionality has not yet been established. Furthermore, tuft cells display variations in function and identity between and within tissues, leading to the delineation of distinct tuft cell populations. As a chemosensory cell type, they display receptors that are responsive to ligands specific for their environment. While many studies have demonstrated the tuft cell response to protists and helminths in the intestine, recent research has highlighted other roles of tuft cells as well as implicated tuft cells in other disease processes including inflammation, cancer, and viral infections. Here, we review the literature on the cytoskeletal structure of tuft cells. Additionally, we focus on new research discussing tuft cell lineage, ligand-receptor interactions, tuft cell tropism, and the role of tuft cells in intestinal disease. Finally, we discuss the implication of tuft cell-targeted therapies in human health and how the morphology of tuft cells may contribute to their functionality.
    MeSH term(s) Humans ; Intestinal Mucosa/metabolism ; Tuft Cells ; Intestines ; Gastrointestinal Tract ; Cell Lineage
    Language English
    Publishing date 2023-10-20
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207933-1
    ISSN 1545-1585 ; 0066-4278
    ISSN (online) 1545-1585
    ISSN 0066-4278
    DOI 10.1146/annurev-physiol-042022-030310
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Brush Border Destruction by Enterohemorrhagic

    Tyska, Matthew J

    Cellular and molecular gastroenterology and hepatology

    2015  Volume 2, Issue 1, Page(s) 7–8

    Language English
    Publishing date 2015-11-25
    Publishing country United States
    Document type Editorial
    ZDB-ID 2819778-1
    ISSN 2352-345X
    ISSN 2352-345X
    DOI 10.1016/j.jcmgh.2015.11.002
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