Results 41 to 50 of about 9,409 (173)

Lis1 activates dynein motility by modulating its pairing with dynactin [PDF]

, 2020
Lissencephaly-1 (Lis1) is a key cofactor for dynein-mediated intracellular transport towards the minus-ends of microtubules. It remains unclear whether Lis1 serves as an inhibitor or an activator of mammalian dynein motility.
Sara Volz, Yildiz, Ahmet, Kusakci, Emre, Mohamed M. Elshenawy, Janina Baumbach, Ahmet Yildiz, Elshenawy, Mohamed M, Volz, Sara, Simon L. Bullock, Bullock, Simon L, Baumbach, Janina, Emre Kusakci   +11 more
core   +1 more source

Cargo-Mediated Activation of Cytoplasmic Dynein in vivo

Frontiers in Cell and Developmental Biology, 2020
Cytoplasmic dynein-1 is a minus-end-directed microtubule motor that transports a variety of cargoes including early endosomes, late endosomes and other organelles.
Xin Xiang, Rongde Qiu
doaj   +1 more source

Adaptor-mediated recruitment of three dyneins to dynactin enhances force generation. [PDF]

Nat Cell Biol
Cytoplasmic dynein is an essential microtubule motor protein that powers organelle transport and mitotic spindle assembly. Its activity depends on dynein–dynactin–cargo adaptor complexes, such as dynein–dynactin–BicD2, which typically function with two ...
Rao L, Liu X, Arnold M, Okada K, McKenney RJ, Stengel K, Sidoli S, Berger F, Gennerich A.   +8 more
europepmc   +2 more sources

Lissencephaly-1 is a context-dependent regulator of the human dynein complex

eLife, 2017
The cytoplasmic dynein-1 (dynein) motor plays a central role in microtubule organisation and cargo transport. These functions are spatially regulated by association of dynein and its accessory complex dynactin with dynamic microtubule plus ends. Here, we
Janina Baumbach, Andal Murthy, Mark A McClintock, Carly I Dix, Ruta Zalyte, Ha Thi Hoang, Simon L Bullock   +6 more
doaj   +1 more source

Cryo-EM shows how dynactin recruits two dyneins for faster movement

, 2017
Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein/dynactin to distinct cargos.
Mohamed M. Elshenawy, Edgar Morales-Rios, Ahmet Yildiz, Linas Urnavicius, Clinton K. Lau, Andrew P. Carter, Carina Motz   +6 more
core   +1 more source

Kazrin promotes dynein/dynactin-dependent traffic from early to recycling endosomes

eLife, 2023
Kazrin is a protein widely expressed in vertebrates whose depletion causes a myriad of developmental defects, in part derived from altered cell adhesion and migration, as well as failure to undergo epidermal to mesenchymal transition.
Ines Hernandez-Perez, Javier Rubio, Adrian Baumann, Henrique Girao, Miriam Ferrando, Elena Rebollo, Anna M Aragay, María Isabel Geli   +7 more
doaj   +1 more source

Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin

, 2022
Cytoplasmic Dynein 1, or Dynein, is a microtubule minus end–directed motor. Dynein motility requires Dynactin and a family of activating adaptors that stabilize the Dynein–Dynactin complex and promote regulated interactions with cargo in space and time ...
Girbig, M., Musacchio, A., d’Amico, Ennio A., Maffini, S., Carter, Andrew P., Maffini, Stefano, Perrakis, Anastassis, Wohlgemuth, Sabine, Ud Din Ahmad, M., Vetter, I., Ud Din Ahmad, Misbha, Müller, F., Musacchio, Andrea, Vetter, Ingrid R., Cmentowski, V., Carter, A., Wohlgemuth, S., Müller, Franziska, Perrakis, A., Girbig, Mathias, Cmentowski, Verena, Janning, Petra, d'Amico, E., Brockmeyer, Andreas, Brockmeyer, A.   +24 more
core   +1 more source

NuMA recruits dynein activity to microtubule minus-ends at mitosis

eLife, 2017
To build the spindle at mitosis, motors exert spatially regulated forces on microtubules. We know that dynein pulls on mammalian spindle microtubule minus-ends, and this localized activity at ends is predicted to allow dynein to cluster microtubules into
Christina L Hueschen, Samuel J Kenny, Ke Xu, Sophie Dumont   +3 more
doaj   +1 more source

Nde1 promotes Lis1-mediated activation of dynein

Nature Communications, 2023
Cytoplasmic dynein drives the motility and force generation functions towards the microtubule minus end. The assembly of dynein with dynactin and a cargo adaptor in an active transport complex is facilitated by Lis1 and Nde1/Ndel1.
Yuanchang Zhao, Sena Oten, Ahmet Yildiz
doaj   +1 more source

SAV1 in Cooperation With FKBP52 Participates in Implantation

Advanced Science, EarlyView.
The MST‐SAV1 complex modulates FKBP52 phosphorylation to fine‐tune PR activity, ensuring timely uterine transition to receptivity under estrogen signaling for implantation. Stromal SAV1 scaffolds MST1/2‐mediated FKBP52 phosphorylation via noncanonical Hippo to promote PR activity.
Yuhan Shao, Yafang Lu, Zhaoyu Jia, Junxiang Ren, Ziyi Ge, Xinyu Liu, Hui Zhao, Zi‐Jiang Chen, Junhao Yan, Wei Wang, Jia Yuan   +10 more
wiley   +1 more source