期刊
JOURNAL OF CELL SCIENCE
卷 130, 期 5, 页码 938-949出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.199091
关键词
Tubulin; Microtubule; Glutamylation; Glycylation; TTLL3; Retina; Photoreceptor; Connecting cilia
类别
资金
- program 'Investissements d'Avenir' [ANR-10-LBX-0038, ANR-10-IDEX-0001-02 PSL]
- Institut Curie (European Commission)
- Fondation pour la Recherche Medicale (FRM) [DEQ20081213977]
- French National Research Agency (ANR) [ANR-12-BSV2-0007]
- Institut National du Cancer (INCA) [2009-1-PL BIO-12-IC-1, 2013-1-PL BIO-02-ICR-1]
- Fondation Pierre Gilles de Gennes (FPGG)
- Retina France
- FRM fellowship [FDT20120925331]
Tubulin is subject to a wide variety of posttranslational modifications, which, as part of the tubulin code, are involved in the regulation of microtubule functions. Glycylation has so far predominantly been found in motile cilia and flagella, and absence of this modification leads to ciliary disassembly. Here, we demonstrate that the correct functioning of connecting cilia of photoreceptors, which are nonmotile sensory cilia, is also dependent on glycylation. In contrast to many other tissues, only one glycylase, TTLL3, is expressed in retina. Ttll3(-/-) mice lack glycylation in photoreceptors, which results in shortening of connecting cilia and slow retinal degeneration. Moreover, absence of glycylation results in increased levels of tubulin glutamylation in photoreceptors, and inversely, the hyperglutamylation observed in the Purkinje cell degeneration (pcd) mouse abolishes glycylation. This suggests that both posttranslational modifications compete for modification sites, and that unbalancing the glutamylation-glycylation equilibrium on axonemes of connecting cilia, regardless of the enzymatic mechanism, invariably leads to retinal degeneration.
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