Work

The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length

Year: 2018

Type: article

Abstract: Axonemal dyneins, including inner dynein arm I1, assemble in the cytoplasm prior to transport into cilia by intraflagellar transport (IFT). How I1 dynein interacts with IFT is not understood. We take advantage of the Chlamydomonas reinhardtii ida3 mutant, which assembles the inner arm I1 dynein complex in the cytoplasm but fails to transport I1 into the cilium, resulting in I1 dynein-deficient axonemes with abnormal motility. The IDA3 gene encodes an ∼115-kDa coiled-coil protein that primarily enters the cilium during ciliary growth but is not an axonemal protein. During growth, IDA3, along with I1 dynein, is transported by anterograde IFT to the tip of the cilium. At the tip, IDA3 uncouples from IFT and diffuses within the cilium. IFT transport of IDA3 decreases as cilia lengthen and subsides once full length is achieved. IDA3 is the first example of an essential and selective IFT adapter that is regulated by ciliary length.

Source: Molecular Biology of the Cell

DOI: 10.1091/mbc.e17-12-0729

Authors: Emily L. Hunter, Karl Lechtreck, Gang Fu, Juyeon Hwang, Huawen Lin, Avanti Gokhale, Lea M. Alford, Brian Lewis, Ryosuke Yamamoto, Ritsu Kamiya, Fan Yang, Daniela Nicastro, Susan K. Dutcher, Maureen Wirschell, Winfield S. Sale

Institutions: Emory University, University of Georgia, The University of Texas Southwestern Medical Center, Washington University in St. Louis, Oglethorpe University, The University of Osaka, Chuo University, University of Mississippi Medical Center

Language: English

Topic: Genetic and Kidney Cyst Diseases

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: American Heart Association, Emory University, Children's Discovery Institute, National Institutes of Health, School of Medicine, Emory University, Japan Society for the Promotion of Science, National Heart, Lung, and Blood Institute, National Institute of General Medical Sciences, National Center for Advancing Translational Sciences

Awards: Functional Substructure of Flagellar Dynein, G3549828030, Atlanta Clinical and Translational Science Institute (ACTSI) Renewal, G6699147628, G7094225672, G7899396192, Functional Substructure of Flagellar Dynein, TRAINING PROGRAM IN BIOCHEMISTRY, CELL AND DEVELOPMENT BIOLOGY, G9000176223, Structure and Function of Complexes that Regulate Ciliary Motility, Georgia Clinical & Translational Science Alliance (Georgia CTSA), Regulation of Motile Cilia Assembly in Lung Disease

OpenAlex ID: W2790725738

FWCI: 2.264

Cites: 67

Cited by: 40

Related to: 10