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  1. Article ; Online: Publisher Correction: Structure of dynein-dynactin on microtubules shows tandem adaptor binding.

    Chaaban, Sami / Carter, Andrew P

    Nature

    2022  Volume 611, Issue 7935, Page(s) E8

    Language English
    Publishing date 2022-08-24
    Publishing country England
    Document type Published Erratum
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-05458-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Structure of dynein-dynactin on microtubules shows tandem adaptor binding.

    Chaaban, Sami / Carter, Andrew P

    Nature

    2022  Volume 610, Issue 7930, Page(s) 212–216

    Abstract: Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo ... ...

    Abstract Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor
    MeSH term(s) Adaptor Proteins, Vesicular Transport/chemistry ; Adaptor Proteins, Vesicular Transport/metabolism ; Adaptor Proteins, Vesicular Transport/ultrastructure ; Cryoelectron Microscopy ; Cytoplasmic Dyneins/chemistry ; Cytoplasmic Dyneins/metabolism ; Cytoplasmic Dyneins/ultrastructure ; Dynactin Complex/chemistry ; Dynactin Complex/metabolism ; Dynactin Complex/ultrastructure ; Microtubules/chemistry ; Microtubules/metabolism ; Microtubules/ultrastructure ; Protein Binding
    Chemical Substances Adaptor Proteins, Vesicular Transport ; Dynactin Complex ; Cytoplasmic Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2022-09-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-05186-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: A microtubule bestiary: structural diversity in tubulin polymers.

    Chaaban, Sami / Brouhard, Gary J

    Molecular biology of the cell

    2017  Volume 28, Issue 22, Page(s) 2924–2931

    Abstract: Microtubules are long, slender polymers of αβ-tubulin found in all eukaryotic cells. Tubulins associate longitudinally to form protofilaments, and adjacent protofilaments associate laterally to form the microtubule. In the textbook view, microtubules are ...

    Abstract Microtubules are long, slender polymers of αβ-tubulin found in all eukaryotic cells. Tubulins associate longitudinally to form protofilaments, and adjacent protofilaments associate laterally to form the microtubule. In the textbook view, microtubules are 1) composed of 13 protofilaments, 2) arranged in a radial array by the centrosome, and 3) built into the 9+2 axoneme. Although these canonical structures predominate in eukaryotes, microtubules with divergent protofilament numbers and higher-order microtubule assemblies have been discovered throughout the last century. Here we survey these noncanonical structures, from the 4-protofilament microtubules of
    Language English
    Publishing date 2017-11-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E16-05-0271
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  4. Article: A force-sensitive mutation reveals a spindle assembly checkpoint-independent role for dynein in anaphase progression.

    Salvador-Garcia, David / Jin, Li / Hensley, Andrew / Gölcük, Mert / Gallaud, Emmanuel / Chaaban, Sami / Port, Fillip / Vagnoni, Alessio / Planelles-Herrero, Vicente José / McClintock, Mark A / Derivery, Emmanuel / Carter, Andrew P / Giet, Régis / Gür, Mert / Yildiz, Ahmet / Bullock, Simon L

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The cytoplasmic dynein-1 (dynein) motor organizes cells by shaping microtubule networks and moving a large variety of cargoes along them. However, dynein's diverse roles ... ...

    Abstract The cytoplasmic dynein-1 (dynein) motor organizes cells by shaping microtubule networks and moving a large variety of cargoes along them. However, dynein's diverse roles complicate
    Language English
    Publishing date 2023-08-04
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.08.03.551815
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Microtubule-associated proteins control the kinetics of microtubule nucleation.

    Wieczorek, Michal / Bechstedt, Susanne / Chaaban, Sami / Brouhard, Gary J

    Nature cell biology

    2015  Volume 17, Issue 7, Page(s) 907–916

    Abstract: Microtubules are born and reborn continuously, even during quiescence. These polymers are nucleated from templates, namely γ-tubulin ring complexes (γ-TuRCs) and severed microtubule ends. Using single-molecule biophysics, we show that nucleation from γ- ... ...

    Abstract Microtubules are born and reborn continuously, even during quiescence. These polymers are nucleated from templates, namely γ-tubulin ring complexes (γ-TuRCs) and severed microtubule ends. Using single-molecule biophysics, we show that nucleation from γ-TuRCs, axonemes and seed microtubules requires tubulin concentrations that lie well above the critical concentration. We measured considerable time lags between the arrival of tubulin and the onset of steady-state elongation. Microtubule-associated proteins (MAPs) alter these time lags. Catastrophe factors (MCAK and EB1) inhibited nucleation, whereas a polymerase (XMAP215) and an anti-catastrophe factor (TPX2) promoted nucleation. We observed similar phenomena in cells. We conclude that GTP hydrolysis inhibits microtubule nucleation by destabilizing the nascent plus ends required for persistent elongation. Our results explain how MAPs establish the spatial and temporal profile of microtubule nucleation.
    MeSH term(s) Animals ; Axoneme/metabolism ; CHO Cells ; Cell Line, Tumor ; Centrosome/metabolism ; Cricetinae ; Cricetulus ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Guanosine Triphosphate/analogs & derivatives ; Guanosine Triphosphate/metabolism ; Humans ; Hydrolysis ; Immunoblotting ; Kinetics ; LLC-PK1 Cells ; Microscopy, Electron ; Microscopy, Fluorescence/methods ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/drug effects ; Microtubules/metabolism ; Microtubules/ultrastructure ; Nocodazole/pharmacology ; Polymerization/drug effects ; Swine ; Tubulin/metabolism ; Tubulin Modulators/pharmacology
    Chemical Substances Microtubule-Associated Proteins ; Tubulin ; Tubulin Modulators ; Green Fluorescent Proteins (147336-22-9) ; 5'-guanylylmethylenebisphosphonate (4E15I11U9B) ; Guanosine Triphosphate (86-01-1) ; Nocodazole (SH1WY3R615)
    Language English
    Publishing date 2015-06-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/ncb3188
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  6. Article ; Online: Crystal structure of human PACRG in complex with MEIG1 reveals roles in axoneme formation and tubulin binding.

    Khan, Nimra / Pelletier, Dylan / McAlear, Thomas S / Croteau, Nathalie / Veyron, Simon / Bayne, Andrew N / Black, Corbin / Ichikawa, Muneyoshi / Khalifa, Ahmad Abdelzaher Zaki / Chaaban, Sami / Kurinov, Igor / Brouhard, Gary / Bechstedt, Susanne / Bui, Khanh Huy / Trempe, Jean-François

    Structure (London, England : 1993)

    2021  Volume 29, Issue 6, Page(s) 572–586.e6

    Abstract: The Parkin co-regulated gene protein (PACRG) binds at the inner junction between doublet microtubules of the axoneme, a structure found in flagella and cilia. PACRG binds to the adaptor protein meiosis expressed gene 1 (MEIG1), but how they bind to ... ...

    Abstract The Parkin co-regulated gene protein (PACRG) binds at the inner junction between doublet microtubules of the axoneme, a structure found in flagella and cilia. PACRG binds to the adaptor protein meiosis expressed gene 1 (MEIG1), but how they bind to microtubules is unknown. Here, we report the crystal structure of human PACRG in complex with MEIG1. PACRG adopts a helical repeat fold with a loop that interacts with MEIG1. Using the structure of the axonemal doublet microtubule from the protozoan Chlamydomonas reinhardtii and single-molecule fluorescence microscopy, we propose that PACRG binds to microtubules while simultaneously recruiting free tubulin to catalyze formation of the inner junction. We show that the homologous PACRG-like protein also mediates dual tubulin interactions but does not bind MEIG1. Our findings establish a framework to assess the function of the PACRG family of proteins and MEIG1 in regulating axoneme assembly.
    MeSH term(s) Axoneme/metabolism ; Binding Sites ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Chlamydomonas reinhardtii/metabolism ; Crystallography, X-Ray ; Humans ; Microfilament Proteins/chemistry ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Microscopy, Fluorescence ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Multiprotein Complexes/chemistry ; Mutation ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Protein Binding ; Protein Conformation ; Protein Domains ; Single Molecule Imaging ; Tubulin/metabolism
    Chemical Substances Cell Cycle Proteins ; MEIG1 protein, human ; Microfilament Proteins ; Molecular Chaperones ; Multiprotein Complexes ; Nuclear Proteins ; PACRG protein, human ; Phosphoproteins ; Tubulin
    Language English
    Publishing date 2021-02-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2021.01.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: The Structure and Dynamics of C. elegans Tubulin Reveals the Mechanistic Basis of Microtubule Growth.

    Chaaban, Sami / Jariwala, Shashank / Hsu, Chieh-Ting / Redemann, Stefanie / Kollman, Justin M / Müller-Reichert, Thomas / Sept, David / Bui, Khanh Huy / Brouhard, Gary J

    Developmental cell

    2018  Volume 47, Issue 2, Page(s) 191–204.e8

    Abstract: The dynamic instability of microtubules is a conserved and fundamental mechanism in eukaryotes. Yet microtubules from different species diverge in their growth rates, lattice structures, and responses to GTP hydrolysis. Therefore, we do not know what ... ...

    Abstract The dynamic instability of microtubules is a conserved and fundamental mechanism in eukaryotes. Yet microtubules from different species diverge in their growth rates, lattice structures, and responses to GTP hydrolysis. Therefore, we do not know what limits microtubule growth, what determines microtubule structure, or whether the mechanisms of dynamic instability are universal. Here, we studied microtubules from the nematode C. elegans, which have strikingly fast growth rates and non-canonical lattices in vivo. Using a reconstitution approach, we discovered that C. elegans microtubules combine intrinsically fast growth with very frequent catastrophes. We solved the structure of C. elegans microtubules to 4.8 Å and discovered sequence divergence in the lateral contact loops, one of which is ordered in C. elegans but unresolved in other species. We provide direct evidence that C. elegans tubulin has a higher free energy in solution and propose a model wherein the ordering of lateral contact loops activates tubulin for growth.
    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/physiology ; Guanosine Triphosphate ; Microtubules/metabolism ; Microtubules/physiology ; Microtubules/ultrastructure ; Models, Molecular ; Structure-Activity Relationship ; Tubulin/metabolism ; Tubulin/physiology
    Chemical Substances Caenorhabditis elegans Proteins ; Tubulin ; Guanosine Triphosphate (86-01-1)
    Language English
    Publishing date 2018-09-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2018.08.023
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  8. Article ; Online: The synthetic diazonamide DZ-2384 has distinct effects on microtubule curvature and dynamics without neurotoxicity.

    Wieczorek, Michal / Tcherkezian, Joseph / Bernier, Cynthia / Prota, Andrea E / Chaaban, Sami / Rolland, Yannève / Godbout, Claude / Hancock, Mark A / Arezzo, Joseph C / Ocal, Ozhan / Rocha, Cecilia / Olieric, Natacha / Hall, Anita / Ding, Hui / Bramoullé, Alexandre / Annis, Matthew G / Zogopoulos, George / Harran, Patrick G / Wilkie, Thomas M /
    Brekken, Rolf A / Siegel, Peter M / Steinmetz, Michel O / Shore, Gordon C / Brouhard, Gary J / Roulston, Anne

    Science translational medicine

    2016  Volume 8, Issue 365, Page(s) 365ra159

    Abstract: Microtubule-targeting agents (MTAs) are widely used anticancer agents, but toxicities such as neuropathy limit their clinical use. MTAs bind to and alter the stability of microtubules, causing cell death in mitosis. We describe DZ-2384, a preclinical ... ...

    Abstract Microtubule-targeting agents (MTAs) are widely used anticancer agents, but toxicities such as neuropathy limit their clinical use. MTAs bind to and alter the stability of microtubules, causing cell death in mitosis. We describe DZ-2384, a preclinical compound that exhibits potent antitumor activity in models of multiple cancer types. It has an unusually high safety margin and lacks neurotoxicity in rats at effective plasma concentrations. DZ-2384 binds the vinca domain of tubulin in a distinct way, imparting structurally and functionally different effects on microtubule dynamics compared to other vinca-binding compounds. X-ray crystallography and electron microscopy studies demonstrate that DZ-2384 causes straightening of curved protofilaments, an effect proposed to favor polymerization of tubulin. Both DZ-2384 and the vinca alkaloid vinorelbine inhibit microtubule growth rate; however, DZ-2384 increases the rescue frequency and preserves the microtubule network in nonmitotic cells and in primary neurons. This differential modulation of tubulin results in a potent MTA therapeutic with enhanced safety.
    Language English
    Publishing date 2016-11-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2518854-9
    ISSN 1946-6242 ; 1946-6234
    ISSN (online) 1946-6242
    ISSN 1946-6234
    DOI 10.1126/scitranslmed.aag1093
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