Molecular mechanism of dynein recruitment to kinetochores by the Rod-Zw10-Zwilch complex and Spindly

The molecular motor dynein concentrates at the kinetochore region of mitotic chromosomes in animals to accelerate spindle microtubule capture and to control spindle checkpoint signaling. In this study, we describe the molecular mechanism used by the Rod-Zw10-Zwilch complex and the adaptor Spindly to...

Celý popis

Uložené v:

Podrobná bibliografia
Vydané v:	The Journal of cell biology Ročník 216; číslo 4; s. 943
Hlavní autori:	Gama, José B, Pereira, Cláudia, Simões, Patrícia A, Celestino, Ricardo, Reis, Rita M, Barbosa, Daniel J, Pires, Helena R, Carvalho, Cátia, Amorim, João, Carvalho, Ana X, Cheerambathur, Dhanya K, Gassmann, Reto
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 03.04.2017
Predmet:	Animals Caenorhabditis elegans - metabolism Caenorhabditis elegans - physiology Carrier Proteins - metabolism Cell Cycle Proteins - metabolism Cell Line, Tumor Chromosomal Proteins, Non-Histone - metabolism Chromosome Segregation - physiology Dynactin Complex - metabolism Dyneins - metabolism HeLa Cells Humans Kinetochores - metabolism Kinetochores - physiology Microtubule-Associated Proteins - metabolism Microtubules - metabolism Microtubules - physiology Mitosis - physiology Spindle Apparatus - metabolism Spindle Apparatus - physiology Spindly kinetochore mitosis RZZ complex BICD2 dynein/dynactin
ISSN:	1540-8140, 1540-8140
On-line prístup:	Zistit podrobnosti o prístupe
Tagy:	Pridať tag Žiadne tagy, Buďte prvý, kto otaguje tento záznam!

Popis
Shrnutí:	The molecular motor dynein concentrates at the kinetochore region of mitotic chromosomes in animals to accelerate spindle microtubule capture and to control spindle checkpoint signaling. In this study, we describe the molecular mechanism used by the Rod-Zw10-Zwilch complex and the adaptor Spindly to recruit dynein to kinetochores in embryos and human cells. We show that Rod's N-terminal β-propeller and the associated Zwilch subunit bind Spindly's C-terminal domain, and we identify a specific Zwilch mutant that abrogates Spindly and dynein recruitment in vivo and Spindly binding to a Rod β-propeller-Zwilch complex in vitro. Spindly's N-terminal coiled-coil uses distinct motifs to bind dynein light intermediate chain and the pointed-end complex of dynactin. Mutations in these motifs inhibit assembly of a dynein-dynactin-Spindly complex, and a null mutant of the dynactin pointed-end subunit p27 prevents kinetochore recruitment of dynein-dynactin without affecting other mitotic functions of the motor. Conservation of Spindly-like motifs in adaptors involved in intracellular transport suggests a common mechanism for linking dynein to cargo.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1540-8140 1540-8140
DOI:	10.1083/jcb.201610108