Journal
JOURNAL OF CELL SCIENCE
Volume 123, Issue 20, Pages 3596-3604Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.075259
Keywords
Dynein; Kinesin 1; LIS1; Aspergillus nidulans; Microtubule plus-end
Categories
Funding
- NIH [GM069527]
- USUHS [RO71GO]
- DGICYT [BIO2009-07281]
- Comunidad de Madrid [S2006-SAL-0246]
- CSIC [I3P]
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Cytoplasmic dynein in filamentous fungi accumulates at microtubule plus-ends near the hyphal tip, which is important for minus-end-directed transport of early endosomes. It was hypothesized that dynein is switched on at the plus-end by cargo association. Here, we show in Aspergillus nidulans that kinesin-1-dependent plus-end localization is not a prerequisite for dynein ATPase activation. First, the Walker A and Walker B mutations in the dynein heavy chain AAA1 domain implicated in blocking different steps of the ATPase cycle cause different effects on dynein localization to microtubules, arguing against the suggestion that ATPase is inactive before arriving at the plus-end. Second, dynein from Delta kinA (kinesin 1) mutant cells has normal ATPase activity despite the absence of dynein plus-end accumulation. In Delta kinA hyphae, dynein localizes along microtubules and does not colocalize with abnormally accumulated early endosomes at the hyphal tip. This is in contrast to the colocalization of dynein and early endosomes in the absence of NUDF/LIS1. However, the Walker B mutation allows dynein to colocalize with the hyphal-tip-accumulated early endosomes in the Delta kinA background. We suggest that the normal ability of dyenin to interact with microtubules as an active minus-end-directed motor demands kinesin-1-mediated plus-end accumulation for effective interactions with early endosomes.
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