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CSPP Is a Ciliary Protein Interacting with Nephrocystin 8 and Required for Cilia Formation
Authors:Sebastian Patzke  Sambra Redick  Abdirashid Warsame  Carlos A Murga-Zamalloa  Hemant Khanna  Stephen Doxsey  Trond Stokke
Institution:Departments of *Radiation Biology and ;Pathology, Institute for Cancer Research, The Norwegian Radium Hospital, N-0310 Oslo, Norway; ;Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605; and ;§Department of Ophthalmology and Visual Sciences, University of Michigan, Ann Arbor, MI 48105
Abstract: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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