RPGRIP1L helps to establish the ciliary gate for entry of proteins

Journal of Cell Science
Huawen LinSusan K Dutcher

Abstract

Mutations in transition zone genes change the composition of the ciliary proteome. We isolated new mutations in RPGRIP1L (denotated as RPG1 in algae) that affect the localization of the transition zone protein NPHP4 in the model organism Chlamydomonas reinhardtii NPHP4 localization is not affected in multiple new intraflagellar transport (IFT) mutants. We compared the proteome of cilia from wild-type and mutants that affect the transition zone (RPGRIP1L) or IFT (IFT172 and DHC1b) by mass spectrometry. The rpg1-1 mutant cilia show the most dramatic increase in cytoplasmic proteins. These nonciliary proteins function in translation, membrane remodeling, ATP production and as chaperonins. These proteins are excluded in isolated cilia from fla11-1 (IFT172) and fla24-1 (DHC1b). Our data support the idea that RPGRIP1L, but not IFT proteins, acts as part of the gate for cytoplasmic proteins. The rpg1-1 cilia lack only a few proteins, which suggests that RPGRIP1L only has a minor role of in the retention of ciliary proteins. The fla11-1 mutant shows the greatest loss/reduction of proteins, and one-third of these proteins have a transmembrane domain. Hence, IFT172 may play a role in the retention of proteins.

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Citations

Dec 31, 2019·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Susan K Dutcher
Dec 12, 2020·Molecular Genetics & Genomic Medicine·Ke NingYang Sun
Feb 13, 2021·International Journal of Molecular Sciences·Hiroki YoshiokaJunichi Iwata
Apr 4, 2021·International Journal of Molecular Sciences·Christine VössingJohn Neidhardt
Feb 25, 2021·Molecular Biology of the Cell·Antonia WiegeringChristoph Gerhardt

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Methods Mentioned

BETA
immunoprecipitation
PCR
transgenic
super-resolution microscopy

Software Mentioned

BLAST
Phytozome
Softsearch

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