Title | Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert syndrome. |
Publication Type | Journal Article |
Year of Publication | 2020 |
Authors | Latour, BL, Van De Weghe, JC, Rusterholz, TDs, Letteboer, SJf, Gomez, A, Shaheen, R, Gesemann, M, Karamzade, A, Asadollahi, M, Barroso-Gil, M, Chitre, M, Grout, ME, van Reeuwijk, J, van Beersum, SEc, Miller, CV, Dempsey, JC, Morsy, H, Bamshad, MJ, Nickerson, DA, Neuhauss, SCf, Boldt, K, Ueffing, M, Keramatipour, M, Sayer, JA, Alkuraya, FS, Bachmann-Gagescu, R, Roepman, R, Doherty, D |
Corporate Authors | University of Washington Center for Mendelian Genomics, Genomics England Research Consortium |
Journal | J Clin Invest |
Volume | 130 |
Issue | 8 |
Pagination | 4423-4439 |
Date Published | 2020 08 03 |
ISSN | 1558-8238 |
Keywords | Abnormalities, Multiple, Acetylation, Animals, Armadillo Domain Proteins, Cerebellum, Cilia, CRISPR-Cas Systems, Disease Models, Animal, Eye Abnormalities, Humans, Kidney Diseases, Cystic, Peptides, Retina, Zebrafish, Zebrafish Proteins |
Abstract | Joubert syndrome (JBTS) is a recessive neurodevelopmental ciliopathy characterized by a pathognomonic hindbrain malformation. All known JBTS genes encode proteins involved in the structure or function of primary cilia, ubiquitous antenna-like organelles essential for cellular signal transduction. Here, we used the recently identified JBTS-associated protein armadillo repeat motif-containing 9 (ARMC9) in tandem-affinity purification and yeast 2-hybrid screens to identify a ciliary module whose dysfunction underlies JBTS. In addition to the known JBTS-associated proteins CEP104 and CSPP1, we identified coiled-coil domain containing 66 (CCDC66) and TOG array regulator of axonemal microtubules 1 (TOGARAM1) as ARMC9 interaction partners. We found that TOGARAM1 variants cause JBTS and disrupt TOGARAM1 interaction with ARMC9. Using a combination of protein interaction analyses, characterization of patient-derived fibroblasts, and analysis of CRISPR/Cas9-engineered zebrafish and hTERT-RPE1 cells, we demonstrated that dysfunction of ARMC9 or TOGARAM1 resulted in short cilia with decreased axonemal acetylation and polyglutamylation, but relatively intact transition zone function. Aberrant serum-induced ciliary resorption and cold-induced depolymerization in ARMC9 and TOGARAM1 patient cell lines suggest a role for this new JBTS-associated protein module in ciliary stability. |
DOI | 10.1172/JCI131656 |
Alternate Journal | J Clin Invest |
PubMed ID | 32453716 |
PubMed Central ID | PMC7410078 |
Grant List | U54 HG006493 / HG / NHGRI NIH HHS / United States U54 HD083091 / HD / NICHD NIH HHS / United States F32 HD095599 / HD / NICHD NIH HHS / United States P50 HD103524 / HD / NICHD NIH HHS / United States / DH / Department of Health / United Kingdom K99 HD100554 / HD / NICHD NIH HHS / United States UM1 HG006493 / HG / NHGRI NIH HHS / United States R01 NS064077 / NS / NINDS NIH HHS / United States |