5lpi
From Proteopedia
Structure of the zinc finger array of Cep104
Structural highlights
Disease[CE104_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Function[CE104_HUMAN] Required for ciliogenesis and for structural integrity at the ciliary tip.[1] Publication Abstract from PubMedCilia are thin cell projections with essential roles in cell motility, fluid movement, sensing, and signaling. They are templated from centrioles that dock against the plasma membrane and subsequently extend their peripheral microtubule array. The molecular mechanisms underpinning cilia assembly are incompletely understood. Cep104 is a key factor involved in cilia formation and length regulation that rides on the ends of elongating and shrinking cilia. It is mutated in Joubert syndrome, a genetically heterogeneous ciliopathy. Here we provide structural and biochemical data that Cep104 contains a tubulin-binding TOG (tumor overexpressed gene) domain and a novel C2HC zinc finger array. Furthermore, we identify the kinase Nek1, another ciliopathy-associated protein, as a potential binding partner of this array. Finally, we show that Nek1 competes for binding to Cep104 with the distal centriole-capping protein CP110. Our data suggest a model for Cep104 activity during ciliogenesis and provide a novel link between Cep104 and Nek1. The Ciliopathy-Associated Cep104 Protein Interacts with Tubulin and Nek1 Kinase.,Al-Jassar C, Andreeva A, Barnabas DD, McLaughlin SH, Johnson CM, Yu M, van Breugel M Structure. 2017 Jan 3;25(1):146-156. doi: 10.1016/j.str.2016.11.014. Epub 2016, Dec 22. PMID:28017521[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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