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Role of the Novel Hsp90 Co-Chaperones in Dynein Arms' Preassembly.


ABSTRACT: The outer and inner dynein arms (ODAs and IDAs) are composed of multiple subunits including dynein heavy chains possessing a motor domain. These complex structures are preassembled in the cytoplasm before being transported to the cilia. The molecular mechanism(s) controlling dynein arms' preassembly is poorly understood. Recent evidence suggests that canonical R2TP complex, an Hsp-90 co-chaperone, in cooperation with dynein axonemal assembly factors (DNAAFs), plays a crucial role in the preassembly of ODAs and IDAs. Here, we have summarized recent data concerning the identification of novel chaperone complexes and their role in dynein arms' preassembly and their association with primary cilia dyskinesia (PCD), a human genetic disorder.

SUBMITTER: Fabczak H 

PROVIDER: S-EPMC6940843 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Role of the Novel Hsp90 Co-Chaperones in Dynein Arms' Preassembly.

Fabczak Hanna H   Osinka Anna A  

International journal of molecular sciences 20191207 24


The outer and inner dynein arms (ODAs and IDAs) are composed of multiple subunits including dynein heavy chains possessing a motor domain. These complex structures are preassembled in the cytoplasm before being transported to the cilia. The molecular mechanism(s) controlling dynein arms' preassembly is poorly understood. Recent evidence suggests that canonical R2TP complex, an Hsp-90 co-chaperone, in cooperation with dynein axonemal assembly factors (DNAAFs), plays a crucial role in the preassem  ...[more]

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