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  1. Artikel ; Online: Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast.

    Varela Salgado, Maritzaida / Adriaans, Ingrid E / Touati, Sandra A / Ibanes, Sandy / Lai-Kee-Him, Joséphine / Ancelin, Aurélie / Cipelletti, Luca / Picas, Laura / Piatti, Simonetta

    Nature communications

    2024  Band 15, Heft 1, Seite(n) 3383

    Abstract: A double septin ring accompanies cytokinesis in yeasts and mammalian cells. In budding yeast, reorganisation of the septin collar at the bud neck into a dynamic double ring is essential for actomyosin ring constriction and cytokinesis. Septin ... ...

    Abstract A double septin ring accompanies cytokinesis in yeasts and mammalian cells. In budding yeast, reorganisation of the septin collar at the bud neck into a dynamic double ring is essential for actomyosin ring constriction and cytokinesis. Septin reorganisation requires the Mitotic Exit Network (MEN), a kinase cascade essential for cytokinesis. However, the effectors of MEN in this process are unknown. Here we identify the F-BAR protein Hof1 as a critical target of MEN in septin remodelling. Phospho-mimicking HOF1 mutant alleles overcome the inability of MEN mutants to undergo septin reorganisation by decreasing Hof1 binding to septins and facilitating its translocation to the actomyosin ring. Hof1-mediated septin rearrangement requires its F-BAR domain, suggesting that it may involve a local membrane remodelling that leads to septin reorganisation. In vitro Hof1 can induce the formation of intertwined septin bundles, while a phosphomimetic Hof1 protein has impaired septin-bundling activity. Altogether, our data indicate that Hof1 modulates septin architecture in distinct ways depending on its phosphorylation status.
    Mesh-Begriff(e) Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Phosphorylation ; Septins/metabolism ; Septins/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae/genetics ; Cytokinesis ; Cell Cycle Proteins/metabolism ; Cell Cycle Proteins/genetics ; Actomyosin/metabolism ; Saccharomycetales/metabolism ; Saccharomycetales/genetics ; Mutation ; Protein Binding ; Microtubule-Associated Proteins
    Chemische Substanzen Saccharomyces cerevisiae Proteins ; Septins (EC 3.6.1.-) ; HOF1 protein, S cerevisiae ; Cell Cycle Proteins ; Actomyosin (9013-26-7) ; Microtubule-Associated Proteins
    Sprache Englisch
    Erscheinungsdatum 2024-04-22
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-47709-3
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: PLK1 plays dual roles in centralspindlin regulation during cytokinesis.

    Adriaans, Ingrid E / Basant, Angika / Ponsioen, Bas / Glotzer, Michael / Lens, Susanne M A

    The Journal of cell biology

    2019  Band 218, Heft 4, Seite(n) 1250–1264

    Abstract: Cytokinesis begins upon anaphase onset. An early step involves local activation of the small GTPase RhoA, which triggers assembly of an actomyosin-based contractile ring at the equatorial cortex. Here, we delineated the contributions of PLK1 and Aurora B ...

    Abstract Cytokinesis begins upon anaphase onset. An early step involves local activation of the small GTPase RhoA, which triggers assembly of an actomyosin-based contractile ring at the equatorial cortex. Here, we delineated the contributions of PLK1 and Aurora B to RhoA activation and cytokinesis initiation in human cells. Knock-down of PRC1, which disrupts the spindle midzone, revealed the existence of two pathways that can initiate cleavage furrow ingression. One pathway depends on a well-organized spindle midzone and PLK1, while the other depends on Aurora B activity and centralspindlin at the equatorial cortex and can operate independently of PLK1. We further show that PLK1 inhibition sequesters centralspindlin onto the spindle midzone, making it unavailable for Aurora B at the equatorial cortex. We propose that PLK1 activity promotes the release of centralspindlin from the spindle midzone through inhibition of PRC1, allowing centralspindlin to function as a regulator of spindle midzone formation and as an activator of RhoA at the equatorial cortex.
    Mesh-Begriff(e) Animals ; Aurora Kinase B/genetics ; Aurora Kinase B/metabolism ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cytokinesis ; Enzyme Activation ; HeLa Cells ; Humans ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/enzymology ; Microtubules/genetics ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Protein Transport ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; Signal Transduction ; Spindle Apparatus/enzymology ; Spindle Apparatus/genetics ; rhoA GTP-Binding Protein/genetics ; rhoA GTP-Binding Protein/metabolism ; Polo-Like Kinase 1
    Chemische Substanzen CYK-4 protein, C elegans ; Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; Microtubule-Associated Proteins ; PRC1 protein, human ; Phosphoproteins ; Proto-Oncogene Proteins ; SPD-1 protein, C elegans ; spindlin ; RHOA protein, human (124671-05-2) ; AURKB protein, human (EC 2.7.11.1) ; Aurora Kinase B (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; rhoA GTP-Binding Protein (EC 3.6.5.2)
    Sprache Englisch
    Erscheinungsdatum 2019-02-06
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201805036
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: MKLP2 Is a Motile Kinesin that Transports the Chromosomal Passenger Complex during Anaphase.

    Adriaans, Ingrid E / Hooikaas, Peter Jan / Aher, Amol / Vromans, Martijn J M / van Es, Robert M / Grigoriev, Ilya / Akhmanova, Anna / Lens, Susanne M A

    Current biology : CB

    2020  Band 30, Heft 13, Seite(n) 2628–2637.e9

    Abstract: During cytokinesis, signals from the anaphase spindle direct the formation and position of a contractile ring at the cell cortex [1]. The chromosomal passenger complex (CPC) participates in cytokinesis initiation by signaling from the spindle midzone and ...

    Abstract During cytokinesis, signals from the anaphase spindle direct the formation and position of a contractile ring at the cell cortex [1]. The chromosomal passenger complex (CPC) participates in cytokinesis initiation by signaling from the spindle midzone and equatorial cortex [2], but the mechanisms underlying the anaphase-specific CPC localization are currently unresolved. Accumulation of the CPC at these sites requires the presence of microtubules and the mitotic kinesin-like protein 2, MKLP2 (KIF20A), a member of the kinesin-6 family [2-7], and this has led to the hypothesis that the CPC is transported along microtubules by MKLP2 [3-5, 7]. However, the structure of the MKLP2 motor domain with its extended neck-linker region suggests that this kinesin might not be able to drive processive transport [8, 9]. Furthermore, experiments in Xenopus egg extracts indicated that the CPC might be transported by kinesin-4, KIF4A [10]. Finally, CPC-MKLP2 complexes might be directly recruited to the equatorial cortex via association with actin and myosin II, independent of kinesin activity [4, 8]. Using microscopy-based assays with purified proteins, we demonstrate that MKLP2 is a processive plus-end directed motor that can transport the CPC along microtubules in vitro. In cells, strong suppression of MKLP2-dependent CPC motility by expression of an MKLP2 P-loop mutant perturbs CPC accumulation at both the spindle midzone and equatorial cortex, whereas a weaker inhibition of MKLP2 motor using Paprotrain mainly affects CPC localization to the equatorial cortex. Our data indicate that control of cytokinesis initiation by the CPC requires its directional MKLP2-dependent transport.
    Mesh-Begriff(e) Anaphase/physiology ; Cytokinesis ; HEK293 Cells ; HeLa Cells ; Humans ; Kinesin/genetics ; Kinesin/metabolism ; Multigene Family ; Protein Transport
    Chemische Substanzen KIF20A protein, human ; Kinesin (EC 3.6.4.4)
    Sprache Englisch
    Erscheinungsdatum 2020-06-04
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2020.04.081
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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