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Palmitoylation of the ciliary GTPase ARL13b is necessary for its stability and its role in cilia formation. | LitMetric

AI Article Synopsis

  • Primary cilia are essential for signaling in mammalian cells, and proteins that traffic to these cilia need a process called palmitoylation, which involves attaching a 16-carbon lipid.
  • The study focused on ARL13b, a palmitoylated protein, revealing that its palmitoylation is crucial for its stability and functional roles within cilia, while another lipid modification called myristoylation can only partially replace it in terms of localization.
  • Researchers suggest that understanding palmitoylation could lead to new ways to manipulate cilia function, potentially impacting cellular processes and therapy strategies.

Article Abstract

Primary cilia are hairlike extensions of the plasma membrane of most mammalian cells that serve specialized signaling functions. To traffic properly to cilia, multiple cilia proteins rely on palmitoylation, the post-translational attachment of a saturated 16-carbon lipid. However, details regarding the mechanism of how palmitoylation affects cilia protein localization and function are unknown. Herein, we investigated the protein ADP-ribosylation factor-like GTPase 13b (ARL13b) as a model palmitoylated ciliary protein. Using biochemical, cellular, and studies, we found that ARL13b palmitoylation occurs in mouse kidneys and that it is required for trafficking to and function within cilia. Myristoylation, a 14-carbon lipid, is shown to largely substitute for palmitoylation with regard to cilia localization of ARL13b, but not with regard to its function within cilia. The functional importance of palmitoylation results in part from a dramatic increase in ARL13b stability, which is not observed with myristoylation. Additional results show that blockade of depalmitoylation slows the degradation of ARL13b that occurs during cilia resorption, raising the possibility that the sensitivity of ARL13b stability to palmitoylation may be exploited by the cell to accelerate degradation of ARL13b by depalmitoylating it. Together, the results show that palmitoylation plays a unique and critical role in controlling the localization, stability, abundance, and thus function of ARL13b. Pharmacological manipulation of protein palmitoylation may be a strategy to alter cilia function.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5663873PMC
http://dx.doi.org/10.1074/jbc.M117.792937DOI Listing

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