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    A global analysis of IFT-A function reveals specialization for transport of membrane-associated proteins into cilia

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    Authors
    Picariello, Tyler
    Brown, Jason M.
    Hou, Yuqing
    Swank, Gregory
    Cochran, Deborah A.
    King, Oliver D.
    Lechtreck, Karl
    Pazour, Gregory J.
    Witman, George B.
    UMass Chan Affiliations
    Witman Lab
    Program in Molecular Medicine
    Department of Neurology
    Division of Cell Biology and Imaging, Department of Radiology
    Document Type
    Journal Article
    Publication Date
    2019-02-11
    Keywords
    BBSome
    Flagella
    GTPases
    Intraflagellar transport
    Jeune asphyxiating thoracic dystrophy (JATD)
    Mainzer-Saldino syndrome (MSS)
    Cell Biology
    Cells
    Cellular and Molecular Physiology
    Congenital, Hereditary, and Neonatal Diseases and Abnormalities
    Genetic Phenomena
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    Abstract
    Intraflagellar transport (IFT), which is essential for the formation and function of cilia in most organisms, is the trafficking of IFT trains (i.e. assemblies of IFT particles) that carry cargo within the cilium. Defects in IFT cause several human diseases. IFT trains contain the complexes IFT-A and IFT-B. To dissect the functions of these complexes, we studied a Chlamydomonas mutant that is null for the IFT-A protein IFT140. The mutation had no effect on IFT-B but destabilized IFT-A, preventing flagella assembly. Therefore, IFT-A assembly requires IFT140. Truncated IFT140, which lacks the N-terminal WD repeats of the protein, partially rescued IFT and supported formation of half-length flagella that contained normal levels of IFT-B but greatly reduced amounts of IFT-A. The axonemes of these flagella had normal ultrastructure and, as investigated by SDS-PAGE, normal composition. However, composition of the flagellar 'membrane+matrix' was abnormal. Analysis of the latter fraction by mass spectrometry revealed decreases in small GTPases, lipid-anchored proteins and cell signaling proteins. Thus, IFT-A is specialized for the import of membrane-associated proteins. Abnormal levels of the latter are likely to account for the multiple phenotypes of patients with defects in IFT140. This article has an associated First Person interview with the first author of the paper.
    Source

    J Cell Sci. 2019 Feb 11;132(3). pii: jcs.220749. doi: 10.1242/jcs.220749. Link to article on publisher's site

    DOI
    10.1242/jcs.220749
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/48335
    PubMed ID
    30659111
    Related Resources

    Link to Article in PubMed

    Rights
    © 2019. Published by The Company of Biologists Ltd. Publisher PDF posted after 12 months as allowed by publisher's author rights policy at https://www.biologists.com/user-licence-1-1/.
    ae974a485f413a2113503eed53cd6c53
    10.1242/jcs.220749
    Scopus Count
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    Radiology Publications
    Witman Lab

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