Non-erythroid beta spectrin interacting proteins and their effects on spectrin tetramerization

Cellular and Molecular Biology Letters

Volumn 16, Issue 4, 2011, Pages 595-609

  Sevinc, Akin ^a   Fung, Leslie W M ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

Brain beta spectrin; Brain proteins; Library screening; Spectrin interacting proteins; Spectrin tetramerization; Yeast three hybrid

Indexed keywords

BINDING PROTEIN; CARRIER PROTEINS AND BINDING PROTEINS; COATOMER PROTEIN; COATOMER PROTEIN COMPLEX SUBUNIT BETA 1; COMPLEMENTARY DNA; GLIOMA TUMOR SUPPRESSOR CANDIDATE REGION GENE 2 PROTEIN; ISOPROTEIN; NONERYTHROID ALPHA SPECTRIN; NONERYTHROID BETA SPECTRIN; NONERYTHROID BETA SPECTRIN C; SPECTRIN; SYNTAXIN BINDING PROTEIN 1; THAP DOMAIN CONTAINING APOPTOSIS ASSOCIATED PROTEIN 3; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; ZINC FINGER PROTEIN 251; ACTIN BINDING PROTEIN; CARRIER PROTEIN; FODRIN; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; DNA LIBRARY; DNA SEQUENCE; MOLECULAR INTERACTION; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS; BINDING SITE; BRAIN; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; CYTOLOGY; CYTOSKELETON; GENE LIBRARY; GENETIC TRANSFECTION; GENETICS; HUMAN; METABOLISM; NERVE CELL; PLASMID; POLYMERIZATION; PROTEIN TERTIARY STRUCTURE; TWO HYBRID SYSTEM;

BINDING SITES; BRAIN; CARRIER PROTEINS; CELL LINE; CYTOSKELETON; GENE LIBRARY; HUMANS; MICROFILAMENT PROTEINS; MODELS, MOLECULAR; NEURONS; PEPTIDE FRAGMENTS; PLASMIDS; POLYMERIZATION; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; TRANSFECTION; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 84855728160     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-011-0025-9     Document Type: Article

References (41)

1. Oh, Y. and Fung, L. W.-M. Brain proteins interacting with the tetramerization region of non-erythroid alpha spectrin. Cell. Mol. Biol. Lett. 12 (2007) 604-620.
2. Marchesi, V. T. and Steers, E. Selective solubilization of a protein component of the red cell membrane. Science159 (1968) 203-204.
3. Hiller, G. and Weber, K. Spectrin is absent in various tissue culture cells. Nature299 (1977) 181-183.
4. Levine, J. and Willard, M. Axonally transported polypeptides associated with the internal periphery of many cells. J. Cell Biol. 90 (1981) 631-643.
5. Lee, J. K., Coyne, R. S., Dubreuil, R. R., Goldstein, L. S. B. and Branton, D. Cell shape and interaction defects in α-spectrin mutants of Drosophila Melanogaster. J. Cell Biol. 123 (1993) 1797-1809.
6. Pinder, J. C. and Baines, A. J. A protein accumulator. Nature406 (2000) 253-254.
7. Djinovic-Carugo, K., Gautel, M., Ylanne, J. and Young, P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett. 513 (2002) 119-123.
8. Gascard, P. and Mohandas, N. New insights into functions of erythroid proteins in nonerythroid cells. Curr. Opin. Hematol. 7 (2000) 123-129.
9. Sridharan, D. M., McMahon, L. W. and Lambert, M. W. αII-spectrin interacts with five groups of functionally important proteins in the nucleus. Cell Biol. Int. 30 (2006) 866-878.
10. Kanda, K., Tanaka, T. and Sobue, K. Calspectin (fodrin or nonerythroid spectrin)-actin interaction: a possible involvement of 4, 1-related protein. Biochem. Biophys. Res. Commun. 140 (1986) 1051-1058.
11. Tsukita, S., Tsukita, S., Ishikawa, H., Kurokawa, M., Morimoto, K., Sobue, K. and Kakiuchi, S. Binding sited of calmodulin and actin on the brain spectrin, calspectin. J. Cell Biol. 97 (1983) 574-578.
12. Sobue, K., Kanda, K. and Kakiuchi, S. Solubilization and partial purification of protein kinase systems from brain membranes that phosphorylate calspectin: a spectrin-like calmodulin-binding protein (fodrin). FEBS Lett. 150 (1982) 185-190.
13. Riederer, B. M., Lopresti, L. L., Krebs, K. E., Zagon, I. S. and Goodman, S. R. Brain spectrin (240/235) and brain spectrin (240/235E): conservation of structure and location within mammalian neural tissue. Brain Res. Bull. 21 (1988) 607-616.
14. Ohara, O., Ohara, R., Yamakawa, H., Nakajima, D. and Nakayama, M. Characterization of a new β-spectrin gene which is predominantly expressed in brain. Mol. Brain Res. 57 (1998) 181-192.
15. Tang, Y., Katuri, V., Iqbal, S., Narayan, T., Wang, Z., Lu, R. S., Mishra, L. and Mishra, B. ELF a beta-spectrin is a neuronal precursor cell marker in developing mammalian brain; structure and organization of the elf/beta-G spectrin gene. Oncogene21 (2002) 5255-5267.
16. Lambert, S. and Bennett, V. Postmitotic expression of ankyrinR and beta R-spectrin in discrete neuronal populations of the rat brain. J. Neurosci. 13 (1993) 3725-3735.
17. Tang, Y., Katuri, V., Dillner, A., Mishra, B., Deng, C.-X. and Mishra, L. Disruption of transforming growth factor-β signaling in ELF β-spectrindeficient mice. Science299 (2003) 574-577.
18. Bennett, V. and Baines, A. J. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 81 (2001) 1353-1392.
19. Norman, K. R. and Moerman, D. G. Alpha spectrin is essential for morphogenesis and body wall muscle formation in Caenorhabditis elegant. J. Cell. Biol. 157 (2002) 665-677.
20. McMahon, K. R., Zhang, P., Sridharan, D. M., Lefferts, J. A. and Lambert, M. W. Knockdown of alpha II spectrin in normal human cells by siRNA leads to chromosomal instability and decreased DNA interstrand cross-link repair. Biochem. Biophys. Res. Commun. 381 (2009) 288-293.
21. DeSilva, T. M., Peng, K.-C., Speicher, K. D. and Speicher, D. W. Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides. Biochemistry31 (1992) 10872-10878.
22. Bignone, P. A., King, M. D., Pinder, J. C. and Baines, A. J. Phosphorylation of a threonine unique to the short C-terminal isoform of betaII-spectrin links regulation of alpha-spectrin interaction to neuritogenesis. J. Biol. Chem. 232 (2007) 888-896.
23. Speicher, D., DeSilva, T., Speicher, K., Ursitti, J., Hembach, P. and Weglarz, L. Location of the human red cell spectrin tetramer binding site and detection of a related "closed" hairpin loop dimer using proteolytic footprinting. J. Biol. Chem. 268 (1993) 4227-4235.
24. Mehboob, S., Luo, B.-H., Fu, W., Johnson, M. E. and Fung, L. W.-M. Conformational studies of the tetramerization site of human erythroid spectrin by cysteine-scanning spin-labeling EPR methods. Biochemistry44 (2005) 15898-15905.
25. Ipsaro, J. J., Harper, S. L., Messick, T. E., Marmorstein, R., Mondragon, A. and Speicher, D. W. Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex. Blood115 (2010) 4843-4852.
26. Song, Y., Antoniou, C., Memic, A., Kay, B. K. and Fung, L. W.-M. Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs. Protein Sci. 20 (2011) 867-879.
27. Antoniou, A., Lam, V. Q. and Fung, L. W.-M. Conformational changes at the tetramerization site of erythroid α-spectrin upon binding β-spectrin: a spin label EPR study. Biochemistry47 (2008) 10765-10772.
28. Song, Y., Pipala, N. H. and Fung, L. W.-M. The L49F mutation in alpha erythroid spectrin induces local disorder in the tetramer association region: fluorescence and molecular dynamics studies of free and bound alpha spectrin. Protein Sci. 18 (2009) 1916-1925.
29. Mehboob, S., Song, Y., Witek, M., Long, F., Santarsiero, B. D., Johnson, M. E. and Fung, L. W.-M. Crystal structure of the nonerythroid α-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation. J. Biol. Chem. 285 (2010) 14572-14587.
30. Mehboob, S., Luo, B.-H., Patel, B. M. and Fung, L. W.-M. αβ spectrin coiled coil association at the tetramerization site. Biochemistry40 (2001) 12457-12464.
31. Mehboob, S., Jacob, J., May, M., Kotula, L., Thiyagarajan, P., Johnson, M. E. and Fung, L. W.-M. Structural analysis of the αN-terminal region of erythroid and nonerythroid spectrins by small-angle X-ray scattering. Biochemistry42 (2003) 14702-14710.
32. Begg, G. E., Morris, M. B. and Ralston G. B. Comparison of the saltdependent self-association of brain and erythroid spectrin. Biochemistry36 (1997) 6977-6985.
33. Sumandea, C. A. and Fung, L. W.-M. Mutational effects at the tetramerization site of nonerythroid alpha spectrin. Mol. Brain Res. 136 (2005) 81-90.
34. Marchler-Bauer, A., Lu, S., Anderson, J. B., Chitsaz, F., Derbyshire M. K., DeWeese-Scott, C., Fong, J. H., Geer, L. Y., Geer, R. C., Gonzales, N. R., Gwadz, M., Hurwitz, D. I., Jackson, J. D., Ke, Z., Lanczycki, C. J., Lu, F., Marchler, G. H., Mullokandov, M., Omelchenko, M. V., Robertson, C. L., Song, J. S., Thanki, N., Yamashita, R. A., Zhang, D., Zhang, N., Zheng, C. and Bryant, S. H. CDD: a conserved domain database for the functional annotation of proteins. Nucleic Acids Res. 39 (2011) D225-D229.
35. Roussigne, M., Kossida, S., Lavigne, A.-C., Clouaire, T., Ecochard, V., Glories, A., Amalric, F. and Girard, J.-P. The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P lelement transposase. Trends Biochem. Sci. 28 (2003) 66-69.
36. Macara, I. G., Baldarelli, R., Field, C. M., Glotzer, M., Hayashi, Y., Hsu, S. C., Kennedy, M. B., Kinoshita, M., Longtine, M., Low, C., Maltais, L. J., McKenzie, L., Mitchison, T. J., Nishikawa, T., Noda, M., Petty, E. M., Peifer, M., Pringle, J. R., Robinson, P. J., Roth, D., Russel, S., Stuhlmann, H., Tanaka, M., Tanaka, R., Trimble, W., Ware, J., Zeleznik-Le, N. J. and Zieger, B. Mammalian septins nomenclature. Mol. Biol. Cell13 (2002) 4141-4143.
37. Peterson, E. A. and Petty, E. M. Conquering the complex world of human septins: implications for health and disease. Clin. Genet. 77 (2010) 511-524.
38. Han, G. A., Malintan, N. T., Collins, B. M., Meunier, F. A. and Sugita, S. Munc18-1 as a key regulator of neurosecretion. J. Neurochem. 115 (2010) 1-10.
39. David, Y., Ziv, T., Admon, A. and Navon, A. The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J. Biol. Chem. 285 (2010) 8595-8604.
40. Ardley, H. C., Moynihan, T. P. Markham, A. F. and Robinson, P. A. Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7. Biochim. Biophys. Acta1491 (2000) 57-64.
41. Good, M. C., Zalatan, J. G. and Lim, W. A. Scaffold proteins: hubs for controlling the flow of cellular information. Science332 (2011) 680-686.