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  1. Article ; Online: Shining light on spindle positioning

    Andrea Serra-Marques / Sophie Dumont

    eLife, Vol

    2018  Volume 7

    Abstract: Optogenetic approaches are leading to a better understanding of the forces that determine the plane of cell division. ...

    Abstract Optogenetic approaches are leading to a better understanding of the forces that determine the plane of cell division.
    Keywords spindle positioning ; cortical pulling forces ; dynein ; NuMA ; optogenetic control ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2018-07-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Concerted action of kinesins KIF5B and KIF13B promotes efficient secretory vesicle transport to microtubule plus ends

    Andrea Serra-Marques / Maud Martin / Eugene A Katrukha / Ilya Grigoriev / Cathelijn AE Peeters / Qingyang Liu / Peter Jan Hooikaas / Yao Yao / Veronika Solianova / Ihor Smal / Lotte B Pedersen / Erik Meijering / Lukas C Kapitein / Anna Akhmanova

    eLife, Vol

    2020  Volume 9

    Abstract: Intracellular transport relies on multiple kinesins, but it is poorly understood which kinesins are present on particular cargos, what their contributions are and whether they act simultaneously on the same cargo. Here, we show that Rab6-positive ... ...

    Abstract Intracellular transport relies on multiple kinesins, but it is poorly understood which kinesins are present on particular cargos, what their contributions are and whether they act simultaneously on the same cargo. Here, we show that Rab6-positive secretory vesicles are transported from the Golgi apparatus to the cell periphery by kinesin-1 KIF5B and kinesin-3 KIF13B, which determine the location of secretion events. KIF5B plays a dominant role, whereas KIF13B helps Rab6 vesicles to reach freshly polymerized microtubule ends, to which KIF5B binds poorly, likely because its cofactors, MAP7-family proteins, are slow in populating these ends. Sub-pixel localization demonstrated that during microtubule plus-end directed transport, both kinesins localize to the vesicle front and can be engaged on the same vesicle. When vesicles reverse direction, KIF13B relocates to the middle of the vesicle, while KIF5B shifts to the back, suggesting that KIF5B but not KIF13B undergoes a tug-of-war with a minus-end directed motor.
    Keywords microtubule ; kinesin ; exocytosis ; vesicle transport ; Rab6 ; MAP7 ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 572
    Language English
    Publishing date 2020-11-01T00:00:00Z
    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: KIF13B establishes a CAV1-enriched microdomain at the ciliary transition zone to promote Sonic hedgehog signalling

    Kenneth B. Schou / Johanne B. Mogensen / Stine K. Morthorst / Brian S. Nielsen / Aiste Aleliunaite / Andrea Serra-Marques / Nicoline Fürstenberg / Sophie Saunier / Albane A. Bizet / Iben R. Veland / Anna Akhmanova / Søren T. Christensen / Lotte B. Pedersen

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Volume 15

    Abstract: The ciliary transition zone (TZ) regulates the protein and membrane composition of the primary cilium. Here the authors identify the kinesin-3 motor protein KIF13B as a regulator of TZ membrane composition that controls the ciliary accumulation of ... ...

    Abstract The ciliary transition zone (TZ) regulates the protein and membrane composition of the primary cilium. Here the authors identify the kinesin-3 motor protein KIF13B as a regulator of TZ membrane composition that controls the ciliary accumulation of Smoothened, which is involved in activation of Sonic hedgehog signalling.
    Keywords Science ; Q
    Language English
    Publishing date 2017-01-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Bicaudal D Family Adaptor Proteins Control the Velocity of Dynein-Based Movements

    Max A. Schlager / Andrea Serra-Marques / Ilya Grigoriev / Laura F. Gumy / Marta Esteves da Silva / Phebe S. Wulf / Anna Akhmanova / Casper C. Hoogenraad

    Cell Reports, Vol 8, Iss 5, Pp 1248-

    2014  Volume 1256

    Abstract: Cargo transport along microtubules is driven by the collective function of microtubule plus- and minus-end-directed motors (kinesins and dyneins). How the velocity of cargo transport is driven by opposing teams of motors is still poorly understood. Here, ...

    Abstract Cargo transport along microtubules is driven by the collective function of microtubule plus- and minus-end-directed motors (kinesins and dyneins). How the velocity of cargo transport is driven by opposing teams of motors is still poorly understood. Here, we combined inducible recruitment of motors and adaptors to Rab6 secretory vesicles with detailed tracking of vesicle movements to investigate how changes in the transport machinery affect vesicle motility. We find that the velocities of kinesin-based vesicle movements are slower and more homogeneous than those of dynein-based movements. We also find that Bicaudal D (BICD) adaptor proteins can regulate dynein-based vesicle motility. BICD-related protein 1 (BICDR-1) accelerates minus-end-directed vesicle movements and affects Rab6 vesicle distribution. These changes are accompanied by reduced axonal outgrowth in neurons, supporting their physiological importance. Our study suggests that adaptor proteins can modulate the velocity of dynein-based motility and thereby control the distribution of transport carriers.
    Keywords Biology (General) ; QH301-705.5
    Subject code 572
    Language English
    Publishing date 2014-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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