The centrosomal recruitment of γ-tubulin and its microtubule nucleation activity is α-fodrin guided

References

• Bornens M. The centrosome in cells and organisms. Science. 2012;335(6067):422–426.
   PubMed Web of Science ®Google Scholar
• Zimmerman W, Sparks CA, Doxsey SJ. Amorphous no longer: the centrosome comes into focus. Curr Opin Cell Biol. 1999;11(1):122–128.
   PubMed Web of Science ®Google Scholar
• Lüders J, Stearns T. Microtubule-Organizing centres: a re-evaluation. Nat Rev Mol Cell Biol. 2007;8(2):161–167.
   PubMed Web of Science ®Google Scholar
• Moritz M, Braunfeld MB, Sedat JW, Alberts B and Agard DA. Microtubule nucleation by γ-tubulin-containing rings in the centrosome. Nature. 1995;378(6557):638–640.
   PubMed Web of Science ®Google Scholar
• Khodjakov A, Rieder CL. The sudden recruitment of γ-tubulin to the centrosome at the onset of mitosis and its dynamic exchange throughout the cell cycle, do not require microtubules. J Cell Biol. 1999;146(3):585–596.
   PubMed Web of Science ®Google Scholar
• Ou Y, Rattner JB. The centrosome in higher organisms: structure, composition, and duplication. Int Rev Cytol. 2004;238:119–182.
   PubMedGoogle Scholar
• Stearns T, Evans L, Kirschner M. γ-Tubulin is a highly conserved component of the centrosome. Cell. 1991;65(5):825–836.
   PubMed Web of Science ®Google Scholar
• Moritz M, Braunfeld MB, Guénebaut V, et al. Structure of the γ-tubulin ring complex: a template for microtubule nucleation. Nat Cell Biol. 2000;2(6):365–370.
   PubMed Web of Science ®Google Scholar
• Doxsey SJ, Stein P, Evans L, et al. Pericentrin, a highly conserved centrosome protein involved in microtubule organization. Cell. 1994;76(4):639–650.
   PubMed Web of Science ®Google Scholar
• Murphy SM, Preble AM, Patel UK, et al. GCP5 and GCP6: two new members of the human γ-tubulin complex. Mol Biol Cell. 2001;12(11):3340–3352.
   PubMed Web of Science ®Google Scholar
• Young A, Dictenberg JB, Purohit A, et al. Cytoplasmic dynein-mediated assembly of pericentrin and γ tubulin onto centrosomes. Mol Biol Cell. 2000;11(6):2047–2056.
   PubMed Web of Science ®Google Scholar
• Delgehyr N, Sillibourne J, Bornens M. Microtubule nucleation and anchoring at the centrosome are independent processes linked by ninein function. J Cell Sci. 2005;118(8):1565–1575.
   PubMed Web of Science ®Google Scholar
• Ou YY, Mack GJ, Zhang M, et al. CEP110 and ninein are located in a specific domain of the centrosome associated with centrosome maturation. J Cell Sci. 2002;115(9):1825–1835.
   PubMed Web of Science ®Google Scholar
• Choi Y-K, Liu P, Sze SK, et al. CDK5RAP2 stimulates microtubule nucleation by the γ-tubulin ring complex. J Cell Biol. 2010;191(6):1089–1095.
   PubMed Web of Science ®Google Scholar
• Jia Y, Fong KW, Choi YK, et al. Dynamic recruitment of CDK5RAP2 to centrosomes requires its association with dynein. PLoS One. 2013;8(7):1–7.
   Web of Science ®Google Scholar
• Lüders J, Patel UK, Stearns T. GCP-WD is a γ-tubulin targeting factor required for centrosomal and chromatin-mediated microtubule nucleation. Nat Cell Biol. 2006;8(2):137–147.
   PubMed Web of Science ®Google Scholar
• Winkelmann JC, Forget BG. Erythroid and nonerythroid spectrins. Blood. 1993;81(12):3173–3185.
   PubMed Web of Science ®Google Scholar
• Shashikala S, Kumar R, Thomas NE, et al. Fodrin in centrosomes: implication of a role of fodrin in the transport of gamma-tubulin complex in brain. PLoS One. 2013;8(10):e76613.
   PubMed Web of Science ®Google Scholar
• Thomas NE, Shashikala S, Sengupta S. Cytoplasmic gamma-tubulin complex from brain contains nonerythroid spectrin. J Cell Biochem. 2010;110(6):1334–1341.
   PubMed Web of Science ®Google Scholar
• Levine J, Willard M. Fodrin: axonally transported polypeptides associated with the internal periphery of many cells. J Cell Biol. 1981;90(3):631–642.
   PubMed Web of Science ®Google Scholar
• Bialkowska K, Saido TC, Fox JEB. SH3 domain of spectrin participates in the activation of Rac in specialized calpain-induced integrin signaling complexes. J Cell Sci. 2005;118(2):381–395.
   PubMed Web of Science ®Google Scholar
• Machnicka B, Grochowalska R, Bogusławska DM, et al. Spectrin-Based skeleton as an actor in cell signaling. Cell Mol Life Sci. 2012;69(2):191–201.
   PubMed Web of Science ®Google Scholar
• McMahon LW, Zhang P, Sridharan DM, et al. Knockdown of αII spectrin in normal human cells by siRNA leads to chromosomal instability and decreased DNA interstrand cross-link repair. Biochem Biophys Res Commun. 2009;381(2):288–293.
   PubMed Web of Science ®Google Scholar
• Metral S, Machnicka B, Bigot S, et al. αII-Spectrin is critical for cell adhesion and cell cycle. J Biol Chem. 2009;284(4):2409–2418.
   PubMed Web of Science ®Google Scholar
• Sreeja JS, John R, Dharmapal D, et al. A fresh look at the structure, regulation, and functions of fodrin. Mol Cell Biol. 2020;40(17):1–16.
   Web of Science ®Google Scholar
• Nellikka RK, Sreeja JS, Dharmapal D, et al. α-fodrin is required for the organization of functional microtubules during mitosis. Cell Cycle. 2019;18(20):2713–2726.
   PubMed Web of Science ®Google Scholar
• Sreeja JS, Nellikka RK, John R, et al. Binding of alpha-fodrin to gamma-tubulin accounts for its role in the inhibition of microtubule nucleation. FEBS Lett. 2019;593(11):1154–1165.
   PubMed Web of Science ®Google Scholar
• Stankewich MC, Cianci CD, Stabach PR, et al. Cell organization, growth, and neural and cardiac development require αII-spectrin. J Cell Sci. 2011;124(23):3956–3966.
   PubMed Web of Science ®Google Scholar
• Compton DA. Spindle assembly in animal cells. Annu Rev Biochem. 2000;69(1):95–114.
   PubMedGoogle Scholar
• Singh P, Thomas GE, Gireesh KK, et al. TACC3 protein regulates microtubule nucleation by affecting γ-tubulin ring complexes. J Biol Chem. 2014;289(46):31719–31735.
   PubMed Web of Science ®Google Scholar
• Sreeja JS, Jyothy A, Sengupta S. α-fodrin in cytoskeletal organization and the activity of certain key microtubule kinesins. Genes (Basel). 2021;12(5):750.
   PubMed Web of Science ®Google Scholar
• Barr AR, Kilmartin JV, Gergely F. CDK5RAP2 functions in centrosome to spindle pole attachment and DNA damage response. J Cell Biol. 2010;189(1):23–39.
   PubMed Web of Science ®Google Scholar
• Chen D, Purohit A, Halilovic E, et al. Centrosomal anchoring of protein kinase C βII by pericentrin controls microtubule organization, spindle function, and cytokinesis. J Biol Chem. 2004;279(6):4829–4839.
   PubMed Web of Science ®Google Scholar
• Dictenberg JB, Zimmerman W, Sparks CA, et al. Pericentrin and γ-tubulin form a protein complex and are organized into a novel lattice at the centrosome. J Cell Biol. 1998;141(1):163–174.
   PubMed Web of Science ®Google Scholar
• Hu H, Sheehan JH, Chazin WJ. The mode of action of centrin. J Biol Chem. 2004;279(49):50895–50903.
   PubMed Web of Science ®Google Scholar
• Khouj EM, Prosser SL, Tada H, et al. Differential requirements for the EF-hand domains of human centrin 2 in primary ciliogenesis and nucleotide excision repair. J Cell Sci. 2019;132(19):jcs228486.
   PubMed Web of Science ®Google Scholar
• Salisbury JL, Suino KM, Busby R, et al. Centrin-2 is required for centriole duplication in mammalian cells. Curr Biol. 2002;12(15):1287–1292.
   PubMed Web of Science ®Google Scholar
• Stemm-Wolf AJ, Morgan G, Giddings THsJr, et al. Basal body duplication and maintenance require one member of the Tetrahymena thermophila centrin gene family. Mol Biol Cell. 2005;16(8):3606–3619.
   PubMed Web of Science ®Google Scholar
• Lin T, Neuner A, Flemming D, et al. MOZART1 and γ-tubulin complex receptors are both required to turn γ-TuSC into an active microtubule nucleation template. J Cell Biol. 2016;215(6):823–840.
   PubMed Web of Science ®Google Scholar
• Paz J, Lüders J. Microtubule-organizing centers: towards a minimal parts list. Trends Cell Biol. 2018;28(3):176–187.
   PubMed Web of Science ®Google Scholar
• Kim S, Rhee K, Toda T. Importance of the CEP215-pericentrin interaction for centrosome maturation during mitosis. PLoS One. 2014;9(1):e87016.
   PubMed Web of Science ®Google Scholar
• Unal S, Alanay Y, Cetin M, et al. Striking hematological abnormalities in patients with microcephalic osteodysplastic primordial dwarfism type II (MOPD II): a potential role of pericentrin in hematopoiesis. Pediatr Blood Cancer. 2014;61(2):302–305. DOI:10.1002/pbc.24783
   PubMed Web of Science ®Google Scholar
• Dammermann A, Merdes A. Assembly of centrosomal proteins and microtubule organization depends on PCM-1. J Cell Biol. 2002;159(2):255–266.
   PubMed Web of Science ®Google Scholar
• Cervenkaa I, Valnohovaa J, Bernatika O, et al. Dishevelled is a NEK2 kinase substrate controlling dynamics of centrosomal linker proteins. Proc Nat Acad Sci. 2016;113(33):9304–9309. DOI:10.1073/pnas.1608783113
   PubMed Web of Science ®Google Scholar