Chemical structure-guided design of dynapyrazoles, cell-permeable dynein inhibitors with a unique mode of action

Autor: Jonathan B Steinman, Cristina C Santarossa, Rand M Miller, Lola S Yu, Anna S Serpinskaya, Hideki Furukawa, Sachie Morimoto, Yuta Tanaka, Mitsuyoshi Nishitani, Moriteru Asano, Ruta Zalyte, Alison E Ondrus, Alex G Johnson, Fan Ye, Maxence V Nachury, Yoshiyuki Fukase, Kazuyoshi Aso, Michael A Foley, Vladimir I Gelfand, James K Chen, Andrew P Carter, Tarun M Kapoor

Publikováno v: eLife, Vol 6 (2017)

Cytoplasmic dyneins are motor proteins in the AAA+ superfamily that transport cellular cargos toward microtubule minus-ends. Recently, ciliobrevins were reported as selective cell-permeable inhibitors of cytoplasmic dyneins. As is often true for firs

Externí odkaz: https://doaj.org/article/8d68f62670e24975998fadfad88f3954

Structure of the dynein-2 complex and its assembly with intraflagellar transport trains

Autor: Katerina Toropova, Anthony J. Roberts, Andrew P. Carter, Aakash Gautam Mukhopadhyay, Ruta Zalyte, Miroslav Mladenov

Publikováno v: Nature structural & molecular biology

Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ce8db09939a90f3c31ff765a5018a59
https://pubmed.ncbi.nlm.nih.gov/31451806

Structure of human cytoplasmic dynein-2 primed for its power stroke

Autor: Andrew P. Carter, Ruta Zalyte, Helgo Schmidt, Linas Urnavicius

Publikováno v: Nature

Members of the dynein family, consisting of cytoplasmic and axonemal isoforms, are motors that move towards the minus ends of microtubules. Cytoplasmic dynein-1 (dynein-1) plays roles in mitosis and cellular cargo transport1, and is implicated in vir

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7faa1555a277956ff66a92e9b5b63ce9
https://doi.org/10.1038/nature14023

Chemical structure-guided design of dynapyrazoles, cell-permeable dynein inhibitors with a unique mode of action

Autor: Kazuyoshi Aso, Mitsuyoshi Nishitani, Alison E. Ondrus, Tarun M. Kapoor, Yoshiyuki Fukase, Rand M. Miller, Ruta Zalyte, Andrew P. Carter, Vladimir I. Gelfand, Maxence V. Nachury, Sachie Morimoto, Alex G. Johnson, Anna S. Serpinskaya, Furukawa Hideki, James K. Chen, Michael Foley, Cristina C. Santarossa, Jonathan B. Steinman, Lola S Yu, Moriteru Asano, Fan Ye, Yuta Tanaka

Publikováno v: eLife, Vol 6 (2017)
Steinman, JB; Santarossa, CC; Miller, RM; Yu, LS; Serpinskaya, AS; Furukawa, H; et al.(2017). Chemical structure-guided design of dynapyrazoles, cell-permeable dynein inhibitors with a unique mode of action. ELIFE, 6. doi: 10.7554/eLife.25174. UCSF: Retrieved from: http://www.escholarship.org/uc/item/0dc2627q
eLife

Cytoplasmic dyneins are motor proteins in the AAA+ superfamily that transport cellular cargos toward microtubule minus-ends. Recently, ciliobrevins were reported as selective cell-permeable inhibitors of cytoplasmic dyneins. As is often true for firs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f741cd44e9adc6065d0caaa6f86ce41
https://elifesciences.org/articles/25174

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

Autor: Andal Murthy, Ruta Zalyte, Mark A McClintock, Ha Thi Hoang, Carly I Dix, Simon L. Bullock, Janina Baumbach

Publikováno v: eLife
eLife, Vol 6 (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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12d5baa9a9919bef3a8bb11bc19ce5a1
http://europepmc.org/articles/PMC5413349