Osmotic Stress Blocks Mobility and Dynamic Regulation of Centriolar Satellites
Abstract
:1. Introduction
1.1. Compositional Heterogeneity of Centriolar Satellites
1.2. Centriolar Satellites and Autophagy
1.3. Centriolar Satellites and the Ubiquitin System
1.4. Centriolar Satellites and Kinases
1.5. Future Perspectives for the Centriolar Satellite Field
2. Materials and Methods
2.1. Plasmids and siRNA
2.2. Cell Culture and Reagents
2.3. Immunochemical Methods
2.4. Immunofluorescence Staining and Microscopy
2.5. Structured Illumination Microscopy
2.6. Analysis of Centriolar Satellite Trajectories
3. Results
3.1. Osmotic Stress Counteracts p38-Mediated Dissolution of Centriolar Satellites
3.2. Sorbitol Does Not Interfere with p38-MK2 Signalling
3.3. High Osmolarity Renders CS Immobile and Insensitive to Disassembly and Redistribution
4. Discussion
5. Conclusions
Supplementary Materials
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
- Balczon, R.; Bao, L.; Zimmer, W.E. PCM-1, A 228-kD centrosome autoantigen with a distinct cell cycle distribution. J. Cell Biol. 1994, 124, 783–793. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kubo, A.; Sasaki, H.; Yuba-Kubo, A.; Tsukita, S.; Shiina, N. Centriolar satellites: Molecular characterization, ATP-dependent movement toward centrioles and possible involvement in ciliogenesis. J. Cell Biol. 1999, 147, 969–980. [Google Scholar] [CrossRef] [PubMed]
- Kubo, A.; Tsukita, S. Non-membranous granular organelle consisting of PCM-1: Subcellular distribution and cell-cycle-dependent assembly/disassembly. J. Cell Sci. 2003, 116, 919–928. [Google Scholar] [CrossRef] [PubMed]
- Dammermann, A.; Merdes, A. Assembly of centrosomal proteins and microtubule organization depends on PCM-1. J. Cell Biol. 2002, 159, 255–266. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tollenaere, M.A.X.; Mailand, N.; Bekker-Jensen, S. Centriolarsatellites: Key mediators of centrosome functions. Cell. Mol. Life Sci. 2015, 72, 11–23. [Google Scholar] [CrossRef] [PubMed]
- Hori, A.; Toda, T. Regulation of centriolar satellite integrity and its physiology. Cell. Mol. Life Sci. 2017, 74, 213–229. [Google Scholar] [CrossRef] [PubMed]
- Bärenz, F.; Mayilo, D.; Gruss, O.J. Centriolar satellites: Busy orbits around the centrosome. Eur. J. Cell Biol. 2011, 90, 983–989. [Google Scholar] [CrossRef] [PubMed]
- Gupta, G.D.; Coyaud, É.; Gonçalves, J.; Mojarad, B.A.; Liu, Y.; Wu, Q.; Gheiratmand, L.; Comartin, D.; Tkach, J.M.; Cheung, S.W.T.; et al. A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface. Cell 2015, 163, 1484–1499. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kim, J.C.; Badano, J.L.; Sibold, S.; Esmail, M.A.; Hill, J.; Hoskins, B.E.; Leitch, C.C.; Venner, K.; Ansley, S.J.; Ross, A.J.; et al. The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression. Nat. Genet. 2004, 36, 462–470. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kodani, A.; Tonthat, V.; Wu, B.; Sütterlin, C. Par6 alpha interacts with the dynactin subunit p150 Glued and is a critical regulator of centrosomal protein recruitment. Mol. Biol. Cell 2010, 21, 3376–3385. [Google Scholar] [CrossRef] [PubMed]
- Kim, J.; Krishnaswami, S.R.; Gleeson, J.G. CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium. Hum. Mol. Genet. 2008, 17, 3796–3805. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Nicolas, L.; Merdes, A. Centriolar satellites prevent uncontrolled degradation of centrosome proteins: A speculative review. Cell Stress 2018, 2, 20–24. [Google Scholar]
- Reiter, J.F.; Leroux, M.R. Genes and molecular pathways underpinning ciliopathies. Nat. Rev. Mol. Cell Biol. 2017, 18, 533–547. [Google Scholar] [CrossRef] [PubMed]
- Lopes, C.A.; Prosser, S.L.; Romio, L.; Hirst, R.A.; O’Callaghan, C.; Woolf, A.S.; Fry, A.M. Centriolar satellites are assembly points for proteins implicated in human ciliopathies, including oral-facial-digital syndrome 1. J. Cell Sci. 2011, 124 Pt 4, 600–612. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chamling, X.; Seo, S.; Searby, C.C.; Kim, G.; Slusarski, D.C.; Sheffield, V.C. The Centriolar Satellite Protein AZI1 Interacts with BBS4 and Regulates Ciliary Trafficking of the BBSome. PLoS Genet. 2014, 10, e1004083. [Google Scholar] [CrossRef] [PubMed]
- Zhang, Y.; Seo, S.; Bhattarai, S.; Bugge, K.; Searby, C.C.; Zhang, Q.; Drack, A.V.; Stone, E.M.; Sheffield, V.C. BBS mutations modify phenotypic expression of CEP290-related ciliopathies. Hum. Mol. Genet. 2014, 23, 40–51. [Google Scholar] [CrossRef] [PubMed]
- Kodani, A.; Yu, T.W.; Johnson, J.R.; Jayaraman, D.; Johnson, T.L.; Al-Gazali, L.; Sztriha, L.; Partlow, J.N.; Kim, H.; Krup, A.L.; et al. Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication. eLife 2015, 4. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tang, Z.; Lin, M.G.; Stowe, T.R.; Chen, S.; Zhu, M.; Stearns, T.; Franco, B.; Zhong, Q. Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites. Nature 2013, 502, 254–257. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Villumsen, B.H.; Danielsen, J.R.; Povlsen, L.; Sylvestersen, K.B.; Merdes, A.; Beli, P.; Yang, Y.-G.; Choudhary, C.; Nielsen, M.L.; Mailand, N.; et al. A new cellular stress response that triggers centriolar satellite reorganization and ciliogenesis. EMBO J. 2013, 32, 3029–3040. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- De Saram, P.; Iqbal, A.; Murdoch, J.N.; Wilkinson, C.J. BCAP is a centriolar satellite protein and inhibitor of ciliogenesis. J. Cell Sci. 2017, 130, 3360–3373. [Google Scholar] [CrossRef] [PubMed]
- Kamiya, A.; Tan, P.L.; Kubo, K.-I.; Engelhard, C.; Ishizuka, K.; Kubo, A.; Tsukita, S.; Pulver, A.E.; Nakajima, K.; Cascella, N.G.; et al. Recruitment of PCM1 to the centrosome by the cooperative action of DISC1 and BBS4: A candidate for psychiatric illnesses. Arch. Gen. Psychiatry 2008, 65, 996–1006. [Google Scholar] [CrossRef] [PubMed]
- Nachury, M.V.; Loktev, A.V.; Zhang, Q.; Westlake, C.J.; Peränen, J.; Merdes, A.; Slusarski, D.C.; Scheller, R.H.; Bazan, J.F.; Sheffield, V.C.; et al. A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis. Cell 2007, 129, 1201–1213. [Google Scholar] [CrossRef] [PubMed]
- Stowe, T.R.; Wilkinson, C.J.; Iqbal, A.; Stearns, T. The centriolar satellite proteins Cep72 and Cep290 interact and are required for recruitment of BBS proteins to the cilium. Mol. Biol. Cell 2012, 23, 3322–3335. [Google Scholar] [CrossRef] [PubMed]
- Lacey, K.R.; Jackson, P.K.; Stearns, T. Cyclin-dependent kinase control of centrosome duplication. Proc. Natl. Acad. Sci. USA 1999, 96, 2817–2822. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Rajagopalan, H.; Lengauer, C. Aneuploidy and cancer. Nature 2004, 432, 338–341. [Google Scholar] [CrossRef] [PubMed]
- Sansregret, L.; Swanton, C. The Role of Aneuploidy in Cancer Evolution. Cold Spring Harb. Perspect. Med. 2017, 7, a028373. [Google Scholar] [CrossRef] [PubMed]
- Li, X.; Song, N.; Liu, L.; Liu, X.; Ding, X.; Song, X.; Yang, S.; Shan, L.; Zhou, X.; Su, D.; et al. USP9X regulates centrosome duplication and promotes breast carcinogenesis. Nat. Commun. 2017, 8, 14866. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Firat-Karalar, E.N.; Rauniyar, N.; Yates, J.R.; Stearns, T. Proximity Interactions among Centrosome Components Identify Regulators of Centriole Duplication. Curr. Biol. 2014, 24, 664–670. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hori, A.; Barnouin, K.; Snijders, A.P.; Toda, T. A non-canonical function of Plk4 in centriolar satellite integrity and ciliogenesis through PCM1 phosphorylation. EMBO Rep. 2016, 17, 326–337. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tollenaere, M.A.X.; Villumsen, B.H.; Blasius, M.; Nielsen, J.C.; Wagner, S.A.; Bartek, J.; Beli, P.; Mailand, N.; Bekker-Jensen, S. P38- and MK2-dependent signalling promotes stress-induced centriolar satellite remodelling via 14-3-3-dependent sequestration of CEP131/AZI1. Nat. Commun. 2015, 6, 10075. [Google Scholar] [CrossRef] [PubMed]
- Wang, G.; Chen, Q.; Zhang, X.; Zhang, B.; Zhuo, X.; Liu, J.; Jiang, Q.; Zhang, C. PCM1 recruits Plk1 to the pericentriolar matrix to promote primary cilia disassembly before mitotic entry. J. Cell Sci. 2013, 126 Pt 6, 1355–1365. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Shearer, R.F.; Frikstad, K.M.; McKenna, J.; McCloy, R.A.; Deng, N.; Burgess, A.; Stokke, T.; Patzke, S.; Saunders, D.N. The E3 ubiquitin ligase UBR5 regulates centriolar satellite stability and primary cilia. Mol. Biol. Cell 2018. [Google Scholar] [CrossRef] [PubMed]
- Löffler, H.; Fechter, A.; Liu, F.Y.; Poppelreuther, S.; Krämer, A. DNA damage-induced centrosome amplification occurs via excessive formation of centriolar satellites. Oncogene 2012, 32, 2963. [Google Scholar] [CrossRef] [PubMed]
- Joachim, J.; Razi, M.; Judith, D.; Wirth, M.; Calamita, E.; Encheva, V.; Dynlacht, B.D.; Snijders, A.P.; O’Reilly, N.; Jefferies, H.B.J.; et al. Centriolar Satellites Control GABARAP Ubiquitination and GABARAP-Mediated Autophagy. Curr. Biol. 2017, 27, 2123–2136.e2127. [Google Scholar] [CrossRef] [PubMed]
- Behrends, C.; Sowa, M.E.; Gygi, S.P.; Harper, J.W. Network organization of the human autophagy system. Nature 2010, 466, 68–76. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Joachim, J.; Tooze, S.A. Centrosome to autophagosome signaling: Specific GABARAP regulation by centriolar satellites. Autophagy 2017, 13, 2113–2114. [Google Scholar] [CrossRef] [PubMed]
- Tozer, S.; Baek, C.; Fischer, E.; Goiame, R.; Morin, X. Differential Routing of Mindbomb1 via Centriolar Satellites Regulates Asymmetric Divisions of Neural Progenitors. Neuron 2017, 93, 542–551.e544. [Google Scholar] [CrossRef] [PubMed]
- Pierfelice, T.; Alberi, L.; Gaiano, N. Notch in the vertebrate nervous system: An old dog with new tricks. Neuron 2011, 69, 840–855. [Google Scholar] [CrossRef] [PubMed]
- Engelender, S.; Sharp, A.H.; Colomer, V.; Tokito, M.K.; Lanahan, A.; Worley, P.; Holzbaur, E.L.; Ross, C.A. Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin. Hum. Mol. Genet. 1997, 6, 2205–2212. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Keryer, G.; Pineda, J.R.; Liot, G.; Kim, J.; Dietrich, P.; Benstaali, C.; Smith, K.; Cordelières, F.P.; Spassky, N.; Ferrante, R.J.; et al. Ciliogenesis is regulated by a huntingtin-HAP1-PCM1 pathway and is altered in Huntington disease. J. Clin. Investig. 2011, 121, 4372–4382. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Puram, S.V.; Kim, A.H.; Ikeuchi, Y.; Wilson-Grady, J.T.; Merdes, A.; Gygi, S.P.; Bonni, A. A CaMKIIβ signaling pathway at the centrosome regulates dendrite patterning in the brain. Nat. Neurosci. 2011, 14, 973–983. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Pampliega, O.; Orhon, I.; Patel, B.; Sridhar, S.; Díaz-Carretero, A.; Beau, I.; Codogno, P.; Satir, B.H.; Satir, P.; Cuervo, A.M. Functional interaction between autophagy and ciliogenesis. Nature 2013, 502, 194–200. [Google Scholar] [CrossRef] [PubMed]
- Dikic, I.; Elazar, Z. Mechanism and medical implications of mammalian autophagy. Nat. Rev. Mol. Cell Biol. 2018, 19, 349–364. [Google Scholar] [CrossRef] [PubMed]
- Wang, L.; Lee, K.; Malonis, R.; Sanchez, I.; Dynlacht, B.D. Tethering of an E3 ligase by PCM1 regulates the abundance of centrosomal KIAA0586/Talpid3 and promotes ciliogenesis. eLife 2016, 5, e12950. [Google Scholar] [CrossRef] [PubMed]
- Singla, V.; Romaguera-Ros, M.; Garcia-Verdugo, J.M.; Reiter, J.F. Ofd1, a human disease gene, regulates the length and distal structure of centrioles. Dev. Cell 2010, 18, 410–424. [Google Scholar] [CrossRef] [PubMed]
- Ferrante, M.I.; Zullo, A.; Barra, A.; Bimonte, S.; Messaddeq, N.; Studer, M.; Dollé, P.; Franco, B. Oral-facial-digital type I protein is required for primary cilia formation and left-right axis specification. Nat. Genet. 2006, 38, 112–117. [Google Scholar] [CrossRef] [PubMed]
- Coene, K.L.M.; Roepman, R.; Doherty, D.; Afroze, B.; Kroes, H.Y.; Letteboer, S.J.F.; Ngu, L.H.; Budny, B.; van Wijk, E.; Gorden, N.T.; et al. OFD1 is mutated in X-linked Joubert syndrome and interacts with LCA5-encoded lebercilin. Am. J. Hum. Genet. 2009, 85, 465–481. [Google Scholar] [CrossRef] [PubMed]
- Akimov, V.; Rigbolt, K.T.G.; Nielsen, M.M.; Blagoev, B. Characterization of ubiquitination dependent dynamics in growth factor receptor signaling by quantitative proteomics. Mol. Biosyst. 2011, 7, 3223–3233. [Google Scholar] [CrossRef] [PubMed]
- Wang, Q.; Tang, Y.; Xu, Y.; Xu, S.; Jiang, Y.; Dong, Q.; Zhou, Y.; Ge, W. The X-linked deubiquitinase USP9X is an integral component of centrosome. J. Biol. Chem. 2017, 292, 12874–12884. [Google Scholar] [CrossRef] [PubMed]
- Cajanek, L.; Glatter, T.; Nigg, E.A. The E3 ubiquitin ligase Mib1 regulates Plk4 and centriole biogenesis. J. Cell Sci. 2015, 128, 1674–1682. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hames, R.S.; Crookes, R.E.; Straatman, K.R.; Merdes, A.; Hayes, M.J.; Faragher, A.J.; Fry, A.M. Dynamic recruitment of Nek2 kinase to the centrosome involves microtubules, PCM-1, and localized proteasomal degradation. Mol. Biol. Cell 2005, 16, 1711–1724. [Google Scholar] [CrossRef] [PubMed]
- Spalluto, C.; Wilson, D.I.; Hearn, T. Evidence for centriolar satellite localization of CDK1 and cyclin B2. Cell Cycle 2013, 12, 1802–1803. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Avidor-Reiss, T.; Gopalakrishnan, J. Building a centriole. Curr. Opin. Cell Biol. 2013, 25, 72–77. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Habedanck, R.; Stierhof, Y.-D.; Wilkinson, C.J.; Nigg, E.A. The Polo kinase Plk4 functions in centriole duplication. Nat. Cell Biol. 2005, 7, 1140–1146. [Google Scholar] [CrossRef] [PubMed]
- Hori, A.; Ikebe, C.; Tada, M.; Toda, T. Msd1/SSX2IP-dependent microtubule anchorage ensures spindle orientation and primary cilia formation. EMBO Rep. 2014, 15, 175–184. [Google Scholar] [CrossRef] [PubMed]
- Bärenz, F.; Inoue, D.; Yokoyama, H.; Tegha-Dunghu, J.; Freiss, S.; Draeger, S.; Mayilo, D.; Cado, I.; Merker, S.; Klinger, M.; et al. The centriolar satellite protein SSX2IP promotes centrosome maturation. J. Cell Biol. 2013, 202, 81–95. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Fu, H.; Subramanian, R.R.; Masters, S.C. 14-3-3 proteins: Structure, function, and regulation. Annu. Rev. Pharmacol. Toxicol. 2000, 40, 617–647. [Google Scholar] [CrossRef] [PubMed]
- Prosser, S.L.; Straatman, K.R.; Fry, A.M. Molecular dissection of the centrosome overduplication pathway in S-phase-arrested cells. Mol. Cell. Biol. 2009, 29, 1760–1773. [Google Scholar] [CrossRef] [PubMed]
- Cuadrado, A.; Nebreda, A.R. Mechanisms and functions of p38 MAPK signalling. Biochem. J. 2010, 429, 403–417. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Vertii, A.; Ivshina, M.; Zimmerman, W.; Hehnly, H.; Kant, S.; Doxsey, S. The Centrosome Undergoes Plk1-Independent Interphase Maturation during Inflammation and Mediates Cytokine Release. Dev. Cell 2016, 37, 377–386. [Google Scholar] [CrossRef] [PubMed]
- Andersen, J.S.; Wilkinson, C.J.; Mayor, T.; Mortensen, P.; Nigg, E.A.; Mann, M. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 2003, 426, 570–574. [Google Scholar] [CrossRef] [PubMed]
- Kim, K.; Rhee, K. The pericentriolar satellite protein CEP90 is crucial for integrity of the mitotic spindle pole. J. Cell Sci. 2011, 124 Pt 3, 338–347. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Oshimori, N.; Li, X.; Ohsugi, M.; Yamamoto, T. Cep72 regulates the localization of key centrosomal proteins and proper bipolar spindle formation. EMBO J. 2009, 28, 2066–2076. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kwon, D.Y.; Dimitriadi, M.; Terzic, B.; Cable, C.; Hart, A.C.; Chitnis, A.; Fischbeck, K.H.; Burnett, B.G. The E3 ubiquitin ligase mind bomb 1 ubiquitinates and promotes the degradation of survival of motor neuron protein. Mol. Biol. Cell 2013, 12, 1863–1871. [Google Scholar] [CrossRef] [PubMed]
- Blasius, M.; Wagner, S.A.; Choudhary, C.; Bartek, J.; Jackson, S.P. A quantitative 14-3-3 interaction screen connects the nuclear exosome targeting complex to the DNA damage response. Genes Dev. 2014, 28, 1977–1982. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Rousseau, S.; Peggie, M.; Campbell, D.G.; Nebreda, A.R.; Cohen, P. Nogo-B is a new physiological substrate for MAPKAP-K2. Biochem. J. 2005, 391 Pt 2, 433–440. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sbalzarini, I.F.; Koumoutsakos, P. Feature point tracking and trajectory analysis for video imaging in cell biology. J. Struct. Biol. 2005, 151, 182–195. [Google Scholar] [CrossRef] [PubMed]
- Kulawik, A.; Engesser, R.; Ehlting, C.; Raue, A.; Albrecht, U.; Hahn, B.; Lehmann, W.D.; Gaestel, M.; Klingmuller, U.; Haussinger, D.; et al. IL-1beta-induced and p38(MAPK)-dependent activation of the mitogen-activated protein kinase-activated protein kinase 2 (MK2) in hepatocytes: Signal transduction with robust and concentration-independent signal amplification. J. Biol. Chem. 2017, 292, 6291–6302. [Google Scholar] [CrossRef] [PubMed]
- Lang, R.; Hammer, M.; Mages, J. DUSP meet immunology: Dual specificity MAPK phosphatases in control of the inflammatory response. J. Immunol. 2006, 177, 7497–7504. [Google Scholar] [CrossRef] [PubMed]
- Kultz, D.; Chakravarty, D. Hyperosmolality in the form of elevated NaCl but not urea causes DNA damage in murine kidney cells. Proc. Natl. Acad. Sci. USA 2001, 98, 1999–2004. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Finan, J.D.; Guilak, F. The effects of osmotic stress on the structure and function of the cell nucleus. J. Cell. Biochem. 2010, 109, 460–467. [Google Scholar] [CrossRef] [PubMed]
- Brocker, C.; Thompson, D.C.; Vasiliou, V. The role of hyperosmotic stress in inflammation and disease. Biomol. Concepts 2012, 3, 345–364. [Google Scholar] [CrossRef] [PubMed]
© 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Share and Cite
Nielsen, J.C.; Nordgaard, C.; Tollenaere, M.A.X.; Bekker-Jensen, S. Osmotic Stress Blocks Mobility and Dynamic Regulation of Centriolar Satellites. Cells 2018, 7, 65. https://doi.org/10.3390/cells7070065
Nielsen JC, Nordgaard C, Tollenaere MAX, Bekker-Jensen S. Osmotic Stress Blocks Mobility and Dynamic Regulation of Centriolar Satellites. Cells. 2018; 7(7):65. https://doi.org/10.3390/cells7070065
Chicago/Turabian StyleNielsen, Julie C., Cathrine Nordgaard, Maxim A. X. Tollenaere, and Simon Bekker-Jensen. 2018. "Osmotic Stress Blocks Mobility and Dynamic Regulation of Centriolar Satellites" Cells 7, no. 7: 65. https://doi.org/10.3390/cells7070065