Cloning, characterization, and chromosomal localization of human supervillin (SVIL)

Genomics

Volumn 52, Issue 3, 1998, Pages 342-351

  Pope, Robert K ^a   Pestonjamasp, Kersi N ^a   Smith, Kelly P ^b   Wulfkuhle, Julia D ^a   Strassel, Christopher P ^a   Lawrence, Jeanne B ^b   Luna, Elizabeth J ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; SUPERVILLIN; UNCLASSIFIED DRUG;

ACTIN FILAMENT; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CHROMOSOME 10P; GENE LOCATION; HUMAN; HUMAN CELL; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; PREDICTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN ISOLATION;

BOVINAE;

EID: 0032531127     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1998.5466     Document Type: Article

References (35)

1. Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J. (1990). Basic local alignment search tool. J. Mol. Biol. 215: 403-410.
2. Arpin, M., Pringault, E., Finidori, J., Garcia, A., Jeltsch, J. M., Vandekerckhove, J., and Louvard, D. (1988). Sequence of human villin: A large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity. J. Cell Biol. 107: 1759-1766.
3. Barkalow, K., and Hartwig, J. H. (1995). The role of actin filament barbed-end exposure in cytoskeletal dynamics and cell motility. Biochem. Soc. Trans. 23: 451-456.
4. Ben-Ze'ev, A. (1997). Cytoskeletal and adhesion proteins as tumor suppressors. Curr. Opin. Cell Biol. 9: 99-108.
5. Bretscher, A., Osborn, M., Wehland, J., and Weber, K. (1981). Villin associates with specific microfilamentous structures as seen by immunofluorescence microscopy on tissue sections and cells microinjected with villin. Exp. Cell Res. 135: 213-219.
6. Bretscher, A., Reczek, D., and Berryman, M. (1997). Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J. Cell Sci. 110: 3011-3018.
7. Burridge, K., and Chrzanowska-Wodnicka, M. (1996). Focal adhesions, contractility, and signaling. Annu. Rev. Cell Dev. Biol. 12: 463-518.
8. Church, G. M., and W. Gilbert. (1984). Genomic sequencing. Proc. Natl. Acad. Sci. USA 81: 1991-1995.
9. de Arruda, M. V., Bazari, H., Wallek, M., and Matsudaira, P. (1992). An actin footprint on villin. Single substitutions in a cluster of basic residues inhibit the actin severing but not capping activity of villin. J. Biol. Chem. 267: 13079-13085.
10. Doering, D. S., and Matsudaira, P. (1996). Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 35: 12677-12685.
11. Farrell, R. E., Jr. (1993). "RNA Methodologies. A Laboratory Guide for Isolation and Characterization," Academic Press, San Diego.
12. Finidori, J., Friederich, E., Kwiatkowski, D. J., Louvard, D. (1992). In vivo analysis of functional domains from villin and gelsolin. J. Cell Biol. 116: 1145-1155.
13. Fox, J. E. (1996). Platelet activation: New aspects. Haemostasis 26(Suppl. 4): 102-131.
14. Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J., and Louvard, D. (1992). An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70: 81-92.
15. Glenney, J. R., Jr., Geisler, N., Kaulfus, P., and Weber, K. (1981). Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization. J. Biol. Chem. 256: 8156-8161.
16. Gumbiner, B. M. (1996). Cell adhesion: The molecular basis of tissue architecture and morphogenesis. Cell 84: 345-357.
17. 2+, KC1, and polyphosphoinositides. J. Biol. Chem. 263: 16738-16743.
18. Johnson, C. V., Singer, R. H., and Lawrence J. B. (1991). Fluorescent detection of nuclear RNA and DNA: Implications for genome organization. Methods Cell Biol. 35: 73-99.
19. Luna, E. J., and Hitt, A. L. (1992). Cytoskeleton-plasma membrane interactions. Science 258: 955-964.
20. Luna, E. J., Pestonjamasp, K. N., Cheney, R. E., Strassel, C. P., Lu, T. H., Chia, C. P., Hitt, A. L., Fechheimer, M., Furthmayr, H., and Mooseker, M. S. (1997). Actin-binding membrane proteins identified by F-actin blot overlays. Soc. Gen. Physiol. Ser. 52: 3-18.
21. Lux, S. E. and Palek, J. (1995). Disorders of the red cell membrane. In "Blood: Principles and Practice of Hematology" (R. I. Handin, S. E. Lux, and T. P. Stossel, Eds.), pp. 1701-1818, Lippincott, Philadelphia.
22. Makalowski, W., Zhang, J., and Boguski, M. S. (1996). Comparative analysis of 1196 orthologous mouse and human full-length mRNA and protein sequences. Genome Res. 6: 846-857.
23. Mandai, K., Nakanishi, H., Satoh, A., Obaishi, H., Wada, M., Nishioka, H., Itoh, M., Mizoguchi, A., Aoki, T., Fujimoto, T., Matsuda, Y., Tsukita, S., and Takai, Y. (1997). Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction. J. Cell Biol. 139: 517-528.
24. Marrs, J. A., and Nelson, W. J. (1996). Cadherin cell adhesion molecules in differentiation and embryogenesis. Int. Rev. Cytol. 165: 159-205.
25. McKnight, C. J., Matsudaira, P. T., and Kim, P. S. (1997). NMR structure of the 35-residue villin headpiece subdomain. Nat. Struct. Biol. 4: 180-184.
26. Pestonjamasp, K. N., Amieva, M. R., Strassel, C. P., Nauseef, W. M., Furthmayr, H., and Luna, E. J. (1995). Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes. Mol. Biol. Cell 6: 247-259.
27. Pestonjamasp, K. N., Pope, R. K., Wulfkuhle, J. D., and Luna, E. J. (1997). Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. J. Cell Biol. 139: 1255-1269.
28. Pope, B., Way, M., Matsudaira, P. T., and Weeds, A. (1994). Characterization of the F-actin binding domains of villin: Classification of F-actin binding proteins into two groups according to their binding sites on actin. FEBS Lett. 338: 58-62.
29. Prasad, R., Gu, Y., Alder, H., Nakamura, T., Canaani, O., Saito, H., Huebner, K., Gale, R. P., Nowell, P. C., Kuriyama, K., Miyazaki, C. M., and Canaani, E. (1993). Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation. Cancer Res. 53: 5624-5628.
30. Ruoslahti, E., and Öbrink, B. (1996). Common principles in cell adhesion. Exp. Cell Res. 227: 1-11.
31. Sheetz, M. P. (1994). Cell migration by graded attachment to substrates and contraction. Semin. Cell Biol. 5: 149-155.
32. Tsukita, S., and Yonemura, S. (1997). ERM (ezrin/radixin/moesin) family: From cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9: 70-75.
33. Trybus, T. M., Burgess, A. C., Wojno, K. J., Glover, T. W., and Macoska, J. A. (1996). Distinct areas of allelic loss on chromosomal regions 10p and 10q in human prostate cancer. Cancer Res. 56: 2263-2267.
34. Wydner, K. L., McNeil, J. A., Lin, F., Worman, H. J., and Lawrence, J. B. (1996). Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization. Genomics 32: 474-478.
35. Yap, A. S., Brieher, W. M., and Gumbiner, B. M. (1997). Molecular and functional analysis of cadherin-based adherens junctions. Annu. Rev. Cell Dev. Biol. 13: 119-146.