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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...

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Detalles Bibliográficos
Autores principales: Patzke, Sebastian, Redick, Sambra, Warsame, Abdirashid, Murga-Zamalloa, Carlos A., Khanna, Hemant, Doxsey, Stephen, Stokke, Trond
Formato: Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2010
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.
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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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