The microtubule regulator EFA-6 forms cortical foci dependent on its intrinsically disordered region and interactions with tubulins.

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  • Additional Information
    • Source:
      Publisher: Cell Press Country of Publication: United States NLM ID: 101573691 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2211-1247 (Electronic) NLM ISO Abbreviation: Cell Rep Subsets: MEDLINE
    • Publication Information:
      Original Publication: [Cambridge, MA] : Cell Press, c 2012-
    • Subject Terms:
      Caenorhabditis elegans*/metabolism ; Caenorhabditis elegans Proteins*/metabolism ; Caenorhabditis elegans Proteins*/genetics ; Guanine Nucleotide Exchange Factors*/metabolism ; Guanine Nucleotide Exchange Factors*/genetics ; Guanine Nucleotide Exchange Factors*/chemistry ; Microtubules*/metabolism ; Tubulin*/metabolism; Animals ; Intrinsically Disordered Proteins/metabolism ; Intrinsically Disordered Proteins/chemistry ; Mutation ; Protein Binding
    • Abstract:
      The EFA6 protein family, originally identified as Sec7 guanine nucleotide exchange factors, has also been found to regulate cortical microtubule (MT) dynamics. Here, we find that in the mature C. elegans epidermal epithelium, EFA-6 forms punctate foci in specific regions of the apical cortex, dependent on its intrinsically disordered region (IDR). The EFA-6 IDR can form biomolecular condensates in vitro. In genetic screens for mutants with altered GFP::EFA-6 localization, we identified a gain-of-function (gf) mutation in α-tubulin tba-1 that induces ectopic EFA-6 foci in multiple cell types. Lethality of tba-1(gf) is partially suppressed by loss of function in efa-6. The ability of TBA-1(gf) to trigger ectopic EFA-6 foci requires β-tubulin TBB-2 and the chaperon EVL-20/Arl2. tba-1(gf)-induced EFA-6 foci display slower turnover, contain the MT-associated protein TAC-1/TACC, and require the EFA-6 MT elimination domain (MTED). Our results reveal functionally important crosstalk between cellular tubulins and cortical MT regulators in vivo.
      Competing Interests: Declaration of interests The authors declare no competing interests.
      (Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved.)
    • Comments:
      Update of: bioRxiv. 2024 Apr 14:2024.04.14.588158. doi: 10.1101/2024.04.14.588158. (PMID: 38645057)
    • Grant Information:
      R01 AG070214 United States AG NIA NIH HHS; R01 AG071591 United States AG NIA NIH HHS
    • Contributed Indexing:
      Keywords: CP: Cell biology; TACC; biomolecular condensates; cortical cytoskeleton; epidermis; microtubule; tubulin heterodimer
    • Accession Number:
      0 (Caenorhabditis elegans Proteins)
      0 (Guanine Nucleotide Exchange Factors)
      0 (Intrinsically Disordered Proteins)
      0 (Tubulin)
      0 (EFA-6 protein, C elegans)
    • Publication Date:
      Date Created: 20240921 Date Completed: 20241025 Latest Revision: 20241215
    • Publication Date:
      20241215
    • Accession Number:
      10.1016/j.celrep.2024.114776
    • Accession Number:
      39305484