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The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone
In differentiated human cells, primary cilia fulfill essential functions in converting mechanical or chemical stimuli into intracellular signals. Formation and maintenance of cilia require multiple functions associated with the centriole-derived basal body, from which axonemal microtubules grow and...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3923641/ https://www.ncbi.nlm.nih.gov/pubmed/24356449 http://dx.doi.org/10.1091/mbc.E13-09-0526 |
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author | Klinger, Maren Wang, Wenbo Kuhns, Stefanie Bärenz, Felix Dräger-Meurer, Stefanie Pereira, Gislene Gruss, Oliver J. |
author_facet | Klinger, Maren Wang, Wenbo Kuhns, Stefanie Bärenz, Felix Dräger-Meurer, Stefanie Pereira, Gislene Gruss, Oliver J. |
author_sort | Klinger, Maren |
collection | PubMed |
description | In differentiated human cells, primary cilia fulfill essential functions in converting mechanical or chemical stimuli into intracellular signals. Formation and maintenance of cilia require multiple functions associated with the centriole-derived basal body, from which axonemal microtubules grow and which assembles a gate to maintain the specific ciliary proteome. Here we characterize the function of a novel centriolar satellite protein, synovial sarcoma X breakpoint–interacting protein 2 (SSX2IP), in the assembly of primary cilia. We show that SSX2IP localizes to the basal body of primary cilia in human and murine ciliated cells. Using small interfering RNA knockdown in human cells, we demonstrate the importance of SSX2IP for efficient recruitment of the ciliopathy-associated satellite protein Cep290 to both satellites and the basal body. Cep290 takes a central role in gating proteins to the ciliary compartment. Consistent with that, loss of SSX2IP drastically reduces entry of the BBSome, which functions to target membrane proteins to primary cilia, and interferes with efficient accumulation of the key regulator of ciliary membrane protein targeting, Rab8. Finally, we show that SSX2IP knockdown limits targeting of the ciliary membrane protein and BBSome cargo, somatostatin receptor 3, and significantly reduces axoneme length. Our data establish SSX2IP as a novel targeting factor for ciliary membrane proteins cooperating with Cep290, the BBSome, and Rab8. |
format | Online Article Text |
id | pubmed-3923641 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-39236412014-04-30 The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone Klinger, Maren Wang, Wenbo Kuhns, Stefanie Bärenz, Felix Dräger-Meurer, Stefanie Pereira, Gislene Gruss, Oliver J. Mol Biol Cell Articles In differentiated human cells, primary cilia fulfill essential functions in converting mechanical or chemical stimuli into intracellular signals. Formation and maintenance of cilia require multiple functions associated with the centriole-derived basal body, from which axonemal microtubules grow and which assembles a gate to maintain the specific ciliary proteome. Here we characterize the function of a novel centriolar satellite protein, synovial sarcoma X breakpoint–interacting protein 2 (SSX2IP), in the assembly of primary cilia. We show that SSX2IP localizes to the basal body of primary cilia in human and murine ciliated cells. Using small interfering RNA knockdown in human cells, we demonstrate the importance of SSX2IP for efficient recruitment of the ciliopathy-associated satellite protein Cep290 to both satellites and the basal body. Cep290 takes a central role in gating proteins to the ciliary compartment. Consistent with that, loss of SSX2IP drastically reduces entry of the BBSome, which functions to target membrane proteins to primary cilia, and interferes with efficient accumulation of the key regulator of ciliary membrane protein targeting, Rab8. Finally, we show that SSX2IP knockdown limits targeting of the ciliary membrane protein and BBSome cargo, somatostatin receptor 3, and significantly reduces axoneme length. Our data establish SSX2IP as a novel targeting factor for ciliary membrane proteins cooperating with Cep290, the BBSome, and Rab8. The American Society for Cell Biology 2014-02-15 /pmc/articles/PMC3923641/ /pubmed/24356449 http://dx.doi.org/10.1091/mbc.E13-09-0526 Text en © 2014 Klinger et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Klinger, Maren Wang, Wenbo Kuhns, Stefanie Bärenz, Felix Dräger-Meurer, Stefanie Pereira, Gislene Gruss, Oliver J. The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone |
title | The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone |
title_full | The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone |
title_fullStr | The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone |
title_full_unstemmed | The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone |
title_short | The novel centriolar satellite protein SSX2IP targets Cep290 to the ciliary transition zone |
title_sort | novel centriolar satellite protein ssx2ip targets cep290 to the ciliary transition zone |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3923641/ https://www.ncbi.nlm.nih.gov/pubmed/24356449 http://dx.doi.org/10.1091/mbc.E13-09-0526 |
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