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Open AccessArticle

Ciliopathy-Associated Protein Kinase ICK Requires Its Non-Catalytic Carboxyl-Terminal Domain for Regulation of Ciliogenesis

1
Department of Pharmacology, University of Virginia Medical School, Charlottesville, VA 22908, USA
2
Department of Microbiology, Immunology, and Cancer Biology, University of Virginia Medical School, Charlottesville, VA 22908, USA
3
Center for Cell Signaling, University of Virginia Medical School, Charlottesville, VA 22908, USA
4
Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI 48109, USA
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Cells 2019, 8(7), 677; https://doi.org/10.3390/cells8070677
Received: 14 June 2019 / Revised: 1 July 2019 / Accepted: 2 July 2019 / Published: 4 July 2019
(This article belongs to the Special Issue Cilia and Flagella: Structure, Function and Beyond)
Loss-of-function mutations in the human ICK (intestinal cell kinase) gene cause dysfunctional primary cilia and perinatal lethality which are associated with human ciliopathies. The enzyme that we herein call CAPK (ciliopathy-associated protein kinase) is a serine/threonine protein kinase that has a highly conserved MAPK-like N-terminal catalytic domain and an unstructured C-terminal domain (CTD) whose functions are completely unknown. In this study, we demonstrate that truncation of the CTD impairs the ability of CAPK to interact with and phosphorylate its substrate, kinesin family member 3A (KIF3A). We also find that deletion of the CTD of CAPK compromises both localization to the primary cilium and negative regulation of ciliogenesis. Thus, CAPK substrate recognition, ciliary targeting, and ciliary function depend on the non-catalytic CTD of the protein which is predicted to be intrinsically disordered. View Full-Text
Keywords: primary cilia; ciliopathy; intestinal cell kinase; ciliopathy-associated protein kinase; ciliogenesis; kinesin family member 3A; and phosphorylation primary cilia; ciliopathy; intestinal cell kinase; ciliopathy-associated protein kinase; ciliogenesis; kinesin family member 3A; and phosphorylation
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MDPI and ACS Style

Oh, Y.S.; Wang, E.J.; Gailey, C.D.; Brautigan, D.L.; Allen, B.L.; Fu, Z. Ciliopathy-Associated Protein Kinase ICK Requires Its Non-Catalytic Carboxyl-Terminal Domain for Regulation of Ciliogenesis. Cells 2019, 8, 677.

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