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Characterization of Aspergillus nidulans DidB Did2, a non-essential component of the multivesicular body pathway.


ABSTRACT: ESCRT-III heteropolymers mediate membrane protein cargo sorting into multivesicular endosomes for subsequent vacuolar degradation. We studied the localization of largely uncharacterized Aspergillus nidulans ESCRT-III using its key structural component Vps32 and the 'associated' component DidB(Did2). Vps32-GFP localizes to motile early endosomes as reported, but predominates in aggregates often associated with vacuoles due to inability to dissociate from endosomes. DidB(Did)(2) regulating Vps4 (the ATPase disassembling ESCRT-III) is not essential. Consistent with this accessory role, didB Delta is unable to block the MVB sorting of the glutamate transporter AgtA, but increases its steady-state level and mislocalizes a fraction of the permease to the plasma membrane under conditions promoting its vacuolar targeting. didB Delta exacerbates the dominant-negative growth defect resulting from Vps32-GFP over-expression. A proportion of DidB-GFP is detectable in early endosomes colocalizing with RabA(Rab5) and accumulating in nudA1 tips, suggesting that ESCRT-III assembles on endosomes from the early steps of the endocytic pathway.

SUBMITTER: Hervas-Aguilar A 

PROVIDER: S-EPMC2884189 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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Characterization of Aspergillus nidulans DidB Did2, a non-essential component of the multivesicular body pathway.

Hervás-Aguilar América A   Rodríguez-Galán Olga O   Galindo Antonio A   Abenza Juan F JF   Arst Herbert N HN   Peñalva Miguel A MA  

Fungal genetics and biology : FG & B 20100401 7


ESCRT-III heteropolymers mediate membrane protein cargo sorting into multivesicular endosomes for subsequent vacuolar degradation. We studied the localization of largely uncharacterized Aspergillus nidulans ESCRT-III using its key structural component Vps32 and the 'associated' component DidB(Did2). Vps32-GFP localizes to motile early endosomes as reported, but predominates in aggregates often associated with vacuoles due to inability to dissociate from endosomes. DidB(Did)(2) regulating Vps4 (t  ...[more]

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