期刊
JOURNAL OF CELL BIOLOGY
卷 204, 期 6, 页码 1009-1026出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201308009
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资金
- National Institutes of Health [R01 GM097580]
- Uniformed Services University intramural grant
- Biotechnology and Biological Sciences Research Council [BB/F01189X/1]
- Wellcome Trust [084660/Z/08/Z]
- Spanish Government [BIO2012-30695]
- Comunidad de Madrid [S2012/BMD2414]
- Wellcome Trust [084660/Z/08/Z] Funding Source: Wellcome Trust
- BBSRC [BB/F01189X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F01189X/1] Funding Source: researchfish
Cytoplasmic dynein transports membranous cargoes along microtubules, but the mechanism of dynein-cargo interaction is unclear. From a genetic screen, we identified a homologue of human Hook proteins, HookA, as a factor required for dynein-mediated early endosome movement in the filamentous fungus Aspergillus nidulans. HookA contains a putative N-terminal microtubule-binding domain followed by coiled-coil domains and a C-terminal cargo-binding domain, an organization reminiscent of cytoplasmic linker proteins. HookA-early endosome interaction occurs independently of dynein-early endosome interaction and requires the C-terminal domain. Importantly, HookA interacts with dynein and dynactin independently of HookA-early endosome interaction but dependent on the N-terminal part of HookA. Both dynein and the p25 subunit of dynactin are required for the interaction between HookA and dynein-dynactin, and loss of HookA significantly weakens dynein-early endosome interaction, causing a virtually complete absence of early endosome movement. Thus, HookA is a novel linker important for dynein-early endosome interaction in vivo.
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