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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Published in:Molecular biology of the cell 2010-08, Vol.21 (15), p.2555-2567
Main Authors: Patzke, Sebastian, Redick, Sambra, Warsame, Abdirashid, Murga-Zamalloa, Carlos A, Khanna, Hemant, Doxsey, Stephen, Stokke, Trond
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - metabolism
Antibody Specificity
Axoneme - metabolism
Bronchi - cytology
Bronchi - metabolism
Cell Cycle
Cell Cycle Proteins - metabolism
Cell Line
Centrioles - metabolism
Cilia - metabolism
Epithelial Cells - cytology
Epithelial Cells - metabolism
Gene Knockdown Techniques
Humans
Kidney - cytology
Kidney - metabolism
Microtubule-Associated Proteins - metabolism
Organogenesis
Protein Binding
Protein Isoforms - metabolism
Protein Stability
Protein Transport
Retina - cytology
Retina - metabolism
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Summary: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.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E09-06-0503