5LPH

Structure of the TOG domain of human Cep104

Summary for 5LPH

• Entry DOI: 10.2210/pdb5lph/pdb
• Descriptor: Centrosomal protein of 104 kDa (2 entities in total)
• Functional Keywords: tog domain, heat repeat, tubulin binding, cep104, basal body, centriole, cilia, cell cycle
• Biological source: Homo sapiens (Human)
• Cellular location: Cell projection, cilium : O60308
• Total number of polymer chains: 2
• Total formula weight: 65180.50

Authors

van Breugel, M. (deposition date: 2016-08-13, release date: 2017-01-11, Last modification date: 2024-10-23)

Primary citation

Al-Jassar, C.,Andreeva, A.,Barnabas, D.D.,McLaughlin, S.H.,Johnson, C.M.,Yu, M.,van Breugel, M.
The Ciliopathy-Associated Cep104 Protein Interacts with Tubulin and Nek1 Kinase.
Structure, 25:146-156, 2017

PubMed Abstract: Cilia 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.

PubMed: 28017521
DOI: 10.1016/j.str.2016.11.014

Experimental method

X-RAY DIFFRACTION (2.25 Å)