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CEP19-RABL2-IFT-B axis controls BBSome-mediated ciliary GPCR export.

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Molecular Biology of the Cell
|September 8, 2022
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Summary

The RABL2 GTPase, when in its GTP-bound state, is crucial for recruiting the intraflagellar transport B (IFT-B) complex to the ciliary base. This recruitment is essential for proper ciliary protein trafficking and preventing Bardet-Biedl syndrome (BBS) related defects.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Intraflagellar transport (IFT) machinery regulates protein movement within cilia.
  • The IFT-B complex and Bardet-Biedl syndrome (BBS) proteins (BBSome) cooperate in ciliary membrane protein export.
  • IFT25-IFT27 serves as a link between the IFT-B complex and the BBSome.

Purpose of the Study:

  • To investigate the interaction between RABL2 GTPase and the IFT-B complex.
  • To elucidate the role of GTP-bound RABL2 in ciliary protein trafficking and BBS pathogenesis.
  • To understand the mechanism of IFT-B complex recruitment to the ciliary base.

Main Methods:

  • Co-immunoprecipitation assays to study protein interactions.
  • Analysis of ciliary protein localization in cells expressing wild-type and mutant RABL2.
  • CRISPR/Cas9 gene editing to create IFT27 knockout cells for comparison.

Main Results:

  • GTP-bound RABL2 binds to the IFT74/BBS22-IFT81 dimer of IFT-B, mutually exclusively with IFT25-IFT27.
  • Expression of GTP-locked RABL2 [RABL2(Q80L)] phenocopies IFT27-knockout cells, causing BBS-associated ciliary defects.
  • RABL2(Q80L) induces accumulation of BBS proteins and ciliary GPCRs, and suppresses their export.
  • RABL2(Q80L) enters cilia dependent on CEP19, but this entry is not required for the observed BBS-like defects.

Conclusions:

  • GTP-bound RABL2 is essential for recruiting the IFT-B complex to the ciliary base.
  • RABL2 acts upstream of IFT25-IFT27 in the ciliary export pathway.
  • Dysregulation of RABL2 GTPase activity contributes to Bardet-Biedl syndrome ciliary defects.