TY - JOUR
T1 - HookA is a novel dynein-early endosome linker critical for cargo movement in vivo
AU - Zhang, Jun
AU - Qiu, Rongde
AU - Arst, Herbert N.
AU - Peñalva, Miguel A.
AU - Xiang, Xin
PY - 2014/3
Y1 - 2014/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84896295630&partnerID=8YFLogxK
U2 - 10.1083/jcb.201308009
DO - 10.1083/jcb.201308009
M3 - Article
C2 - 24637327
AN - SCOPUS:84896295630
SN - 0021-9525
VL - 204
SP - 1009
EP - 1026
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 6
ER -