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CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation
We described previously the cell cycle- and microtubule-related functions of two splice isoforms of the centrosome spindle pole-associated protein (CSPP and CSPP-L). Here, we show that endogenous CSPP isoforms not only localize to centrosomes and the midbody in cycling cells but also extend to the c...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2912343/ https://www.ncbi.nlm.nih.gov/pubmed/20519441 http://dx.doi.org/10.1091/mbc.E09-06-0503 |
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author | Patzke, Sebastian Redick, Sambra Warsame, Abdirashid Murga-Zamalloa, Carlos A. Khanna, Hemant Doxsey, Stephen Stokke, Trond |
author_facet | Patzke, Sebastian Redick, Sambra Warsame, Abdirashid Murga-Zamalloa, Carlos A. Khanna, Hemant Doxsey, Stephen Stokke, Trond |
author_sort | Patzke, Sebastian |
collection | PubMed |
description | We described previously the cell cycle- and microtubule-related functions of two splice isoforms of the centrosome spindle pole-associated protein (CSPP and CSPP-L). Here, we show that endogenous CSPP isoforms not only localize to centrosomes and the midbody in cycling cells but also extend to the cilia axoneme in postmitotic resting cells. They are required for ciliogenesis in hTERT-RPE1 cells in vitro and are expressed in ciliated renal, retinal, and respiratory cells in vivo. We report that CSPP isoforms require their common C-terminal domain to interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary complex with NPHP8 and NPHP4. We find CSPP-L to be required for the efficient localization of NPHP8 but not NPHP4 to the basal body. The ciliogenesis defect in hTERT-RPE1 cells is, however, not mediated through loss of NPHP8. Similar to the effects of ectopical expression of CSPP-L, cilia length increased in NPHP8-depleted cells. Our results thus suggest that CSPP proteins may be involved in further cytoskeletal organization of the basal body and its primary cilium. To conclude, we have identified a novel, nonmitotic function of CSPP proteins placing them into a ciliary protein network crucial for normal renal and retinal tissue architecture and physiology. |
format | Text |
id | pubmed-2912343 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-29123432010-10-16 CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation Patzke, Sebastian Redick, Sambra Warsame, Abdirashid Murga-Zamalloa, Carlos A. Khanna, Hemant Doxsey, Stephen Stokke, Trond Mol Biol Cell Articles We described previously the cell cycle- and microtubule-related functions of two splice isoforms of the centrosome spindle pole-associated protein (CSPP and CSPP-L). Here, we show that endogenous CSPP isoforms not only localize to centrosomes and the midbody in cycling cells but also extend to the cilia axoneme in postmitotic resting cells. They are required for ciliogenesis in hTERT-RPE1 cells in vitro and are expressed in ciliated renal, retinal, and respiratory cells in vivo. We report that CSPP isoforms require their common C-terminal domain to interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary complex with NPHP8 and NPHP4. We find CSPP-L to be required for the efficient localization of NPHP8 but not NPHP4 to the basal body. The ciliogenesis defect in hTERT-RPE1 cells is, however, not mediated through loss of NPHP8. Similar to the effects of ectopical expression of CSPP-L, cilia length increased in NPHP8-depleted cells. Our results thus suggest that CSPP proteins may be involved in further cytoskeletal organization of the basal body and its primary cilium. To conclude, we have identified a novel, nonmitotic function of CSPP proteins placing them into a ciliary protein network crucial for normal renal and retinal tissue architecture and physiology. The American Society for Cell Biology 2010-08-01 /pmc/articles/PMC2912343/ /pubmed/20519441 http://dx.doi.org/10.1091/mbc.E09-06-0503 Text en © 2010 by The American Society for Cell Biology |
spellingShingle | Articles Patzke, Sebastian Redick, Sambra Warsame, Abdirashid Murga-Zamalloa, Carlos A. Khanna, Hemant Doxsey, Stephen Stokke, Trond CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation |
title | CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation |
title_full | CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation |
title_fullStr | CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation |
title_full_unstemmed | CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation |
title_short | CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation |
title_sort | cspp is a ciliary protein interacting with nephrocystin 8 and required for cilia formation |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2912343/ https://www.ncbi.nlm.nih.gov/pubmed/20519441 http://dx.doi.org/10.1091/mbc.E09-06-0503 |
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