Protein 4.1R regulates interphase microtubule organization at the centrosome

Journal of Cell Science

Volumn 117, Issue 25, 2004, Pages 6197-6206

  Pérez Ferreiro, Carmen M ^a   Vernos, Isabelle ^b   Correas, Isabel ^a  

^a UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Centrosome; Microtubules; Protein 4.1R

Indexed keywords

ACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; ERYTHROCYTE BAND 4.1 PROTEIN; GAMMA TUBULIN; GLUTATHIONE TRANSFERASE; ISOPROTEIN;

ANIMAL CELL; ARTICLE; CELL SEPARATION; CELLULAR DISTRIBUTION; CENTROSOME; CONFOCAL MICROSCOPY; CONTROLLED STUDY; CYTOARCHITECTURE; DEPOLYMERIZATION; FIBROBLAST; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IN VITRO STUDY; INTERPHASE; MICROTUBULE ASSEMBLY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; WESTERN BLOTTING;

ACTINS; ANIMALS; BLOOD PROTEINS; BLOTTING, WESTERN; CELL LINE, TUMOR; CENTROSOME; CLONING, MOLECULAR; COS CELLS; CYTOSKELETON; DNA, COMPLEMENTARY; DYNEIN ATPASE; ERYTHROCYTES; FIBROBLASTS; GLUTATHIONE TRANSFERASE; HUMANS; INTERPHASE; MICROSCOPY, CONFOCAL; MICROSCOPY, FLUORESCENCE; MICROTUBULE-ASSOCIATED PROTEINS; MICROTUBULES; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; TRANSFECTION; TUBULIN;

ANIMALIA; ASTER;

EID: 12344253237     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01544     Document Type: Article

References (41)

1. Anderson, R. A., Correas, I., Mazzucco, C., Castle, J. D. and Marchesi, V. T. (1988). Tissue-specific analogues of erythrocyte protein 4.1 retain functional domains. J. Cell. Biochem. 37, 269-284.
2. Baklouti, F., Huang, S. C., Vulliamy, T. J., Delaunay, J. and Benz, E. J., Jr (1997). Organization of be human protein 4.1 genomic locus: new insights into the tissue-specific alternative splicing of the pre-mRNA. Genomics 39, 289-302.
3. Bornens, M. (2002). Centrosome composition and microtubule anchoring mechanisms. Curr. Opin. Cell Biol. 14, 25-34.
4. Burkhardt, J. K., Echeverri, C. J., Nilsson, T. and Vallee, R. B. (1997). Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139, 469-484.
5. Clark, I. B. and Meyer, D. I. (1999). Overexpression of normal and mutant Arp1alpha (centractin) differentially affects microtubule organization during mitosis and interphase. J. Cell Sci. 112, 3507-3518.
6. Cohen, A. R., Woods, D. F., Marfatia, S. M., Walther, Z., Chishti, A. H., Anderson, J. M. and Wood, D. F. (1998). Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. J. Cell Biol. 142, 129-138.
7. Conboy, J. (1993). Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. Semin. Hematol. 30, 58-73.
8. Conboy, J. (1999). The role of alternative pre-mRNA splicing in regulating the structure and function of skeletal protein 4.1. Proc. Soc. Exp. Biol. Med. 220, 73-78.
9. Conboy, J. G., Chan, J. Y., Chasis, J. A., Kan, Y. W. and Mohandas, N. (1991). Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1. J. Biol. Chem. 266, 8273-8280.
10. Correas, I. and Avila, J. (1988). Erythrocyte protein 4.1 associates with tubulin. Biochem. J. 255, 217-221.
11. Correas, I., Speicher, D. W. and Marchesi, V. T. (1986). Structure of the spectrin-actin binding site of erythrocyte protein 4.1. J. Biol. Chem. 261, 13362-13366.
12. Chasis, J. A., Coulombel, L., Conboy, J., McGee, S., Andrews, K., Kan, Y. W. and Mohandas, N. (1993). Differentiation-associated switches in protein 4.1 expression. Synthesis of multiple structural isoforms during normal human erythropoiesis. J. Clin. Invest. 91, 329-338.
13. Dammermann, A. and Merdes, A. (2002). Assembly of centrosomal proteins and microtubule organization depends on PCM-1. J. Cell Biol. 159, 255-266.
14. Dammermann, A., Desai, A. and Oegema, K. (2003). The minus end in sight. Curr. Biol. 13, R614-R624.
15. De Cárcer, G., Lallena, M. J. and Correas, I. (1995). Protein 4.1 is a component of the nuclear matrix of mammalian cells. Biochem. J. 312, 871-877.
16. Doxsey, S. (2001). Re-evaluating centrosome function. Nat. Rev. Mol. Cell Biol. 2, 688-698.
17. Echeverri, C. J., Paschal, B. M., Vaughan, K. T. and Vallee, R. B. (1996). Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. J. Cell Biol. 132, 617-633.
18. Gascard, P., Lee, G., Coulombel, L., Auffray, I., Lum, M., Parra, M., Conboy, J. G., Mohandas, N. and Chasis, J. A. (1998). Characterization of multiple isoforms of protein 4.1R expressed during erythroid terminal differentiation. Blood 92, 4404-4414.
19. Hou, V. C. and Conboy, J. G. (2001). Regulation of alternative pre-mRNA splicing during erythroid differentiation. Curr. Opin. Hematol. 8, 74-79.
20. Hou, C. L., Tang, C., Roffler, S. R. and Tang, T. K. (2000). Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translation apparatus. Blood 96 747-753.
21. Hung, L. Y., Tang, C. J. and Tang, T. K. (2000). Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the γ-tubulin complex. Mol. Cell. Biol. 20 7813-7825.
22. Kontrogianni-Konstantopoulos, A., Huang, S. C. and Benz, E. J., Jr (2000). A nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibers. Mol. Biol. Cell 11, 3805-3817.
23. Kontrogianni-Konstantopoulos, A., Frye, C. S., Benz, E. J., Jr and Huang, S. C. (2001). The prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formation. J. Biol. Chem. 276, 20679-20687.
24. Krauss, S. W., Chasis, J. A., Rogers, C., Mohandas, N., Krockmalnic, G. and Penman, S. (1997). Structural protein 4.1 is located in mammalian centrosomes. Proc. Natl. Acad. Sci. USA 94 7297-7302.
25. Krauss, S. W., Heald, R., Lee, G., Nunomura, W., Gimm, J. A., Mohandas, N. and Chasis, J. A. (2002). Two distinct domains of protein 4.1 critical for assembly of functional nuclei in vitro. J. Biol. Chem. 277, 44339-44346.
26. Lallena, M. J. and Correas, I. (1997). Transcription-dependent redistribution of nuclear protein 4.1 to SC35-enriched nuclear domains. J. Cell Sci. 110, 239-247.
27. Lallena, M. J., Martínez, C., Valcárcel, J. and Correas, I. (1998). Functional association of nuclear protein 4.1 with pre-mRNA splicing factors. J. Cell Sci. 111, 1963-1971.
28. Luque, C. M. and Correas, I. (2000). A constitutive region is responsible for nuclear targeting of 4.1R: modulation by alternative sequences results in differential intracellular localization. J. Cell Sci. 113, 2485-2495.
29. Luque, C. M., Lallena, M. J., Pérez-Ferreiro, C. M., de Isidro, Y., de Cárcer, G., Alonso, M. A. and Correas, I. (1999). The N-terminal 209-aa domain of high molecular-weight 4.1R isoforms abrogates 4.1R targeting to the nucleus. Proc. Natl. Acad. Sci. USA 96, 14925-14930.
30. Luque, C. M., Perez-Ferreiro, C. M., Perez-Gonzalez, A., Englmeier, L., Koffa, M. D. and Correas, I. (2003). An alternative domain containing a leucine-rich sequence regulates nuclear cytoplasmic localization of protein 4.1R. J. Biol. Chem. 278, 2686-2691.
31. Mattagajasingh, S. N., Huang, S. C., Hartenstein, J. S., Snyder, M., Marchesi, V. T. and Benz, E. J. (1999). A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein. J. Cell Biol. 145, 29-43.
32. Mattagajasingh, S. N., Huang, S. C., Hartenstein, J. S. and Benz, E. J., Jr (2000). Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton. J. Biol. Chem. 275, 30573-30585.
33. Mitchison, T. and Kirschner, M. (1984). Microtubule assembly nucleated by isolated centrosomes. Nature 312, 232-237.
34. Moudjou, M. and Bornens, M. (1998). Method of centrosome isolation from cultured animal cells. In Cell Biology: A Laboratory Handbook (ed. J. E. Celis), pp. 111-119. London, UK: Academic Press.
35. 2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction. J. Biol. Chem. 272, 30322-30328.
36. Glued and a novel actin. J. Biol. Chem. 268, 15318-15323.
37. Perez-Ferreiro, C. M., Luque, C. M. and Correas, I. (2001). 4.1R proteins associate with interphase microtubules in human T cells: a 4.1R constitutive region is involved in tubulin binding. J. Biol. Chem. 276, 44785-44791.
38. Quintyne, N. J., Gill, S. R., Eckley, D. M., Crego, C. L., Compton, D. A. and Schroer, T. A. (1999). Dynactin is required for microtubule anchoring at centrosomes. J. Cell Biol. 147, 321-334.
39. Schischmanoff, P. O., Yaswen, P., Parra, M. K., Lee, G., Chasis, J. A., Mohandas, N. and Conboy, J. G. (1997). Cell shape-dependent regulation of protein 4.1 alternative pre-mRNA splicing in mammary epithelial cells. J. Biol. Chem. 272, 10254-10259.
40. Tang, T. K., Qin, Z., Leto, T., Marchesi, V. T. and Benz, E. J., Jr (1990). Heterogeneity of mRNA and protein products arising from the protein 4.1 gene in erythroid and nonerythroid tissues. J. Cell Biol. 110, 617-624.
41. Glued. J. Cell Biol. 131, 1507-1516.