The β1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 47, 2005, Pages 17219-17224

  Schredelseker, Johann ^a   Di Biase, Valentina ^b   Obermair, Gerald J ^a   Felder, E Tatiana ^a   Flucher, Bernhard E ^a   Franzini Armstrong, Clara ^b   Grabner, Manfred ^a  

^a INNSBRUCK MEDICAL UNIVERSITY   (Austria)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Calcium channels; Excitation contraction coupling; Tetrads; Zebrafish

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; 1,4 DIHYDROPYRIDINE RECEPTOR BETA1A; CALCIUM ION; COMPLEMENTARY DNA; PROTEIN SUBUNIT; RYANODINE RECEPTOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CALCIUM TRANSPORT; CELL JUNCTION; CELL MEMBRANE; CONTROLLED STUDY; DEPOLARIZATION; DNA SEQUENCE; FREEZE FRACTURE; GENE MUTATION; GENETIC TRANSCRIPTION; HATCHING; IMMUNOCYTOCHEMISTRY; MUSCLE CONTRACTION; MUSCLE EXCITATION; MYOTUBE; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN TARGETING; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SKELETAL MUSCLE; ZEBRA FISH;

ANIMALS; CALCIUM CHANNELS, L-TYPE; GENOTYPE; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; PHENOTYPE; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL; ZEBRAFISH;

ANIMALIA; DANIO RERIO;

EID: 28044446525     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0508710102     Document Type: Article

References (36)

1. Armstrong, C. M., Bezanilla, F. M. & Horowicz, P. (1972) Biochim. Biophys. Acta 267, 605-608.
2. Schneider, M. F. & Chandler, W. K. (1973) Nature 242, 244-246.
3. Rios, E. & Brum, G. (1987) Nature 325, 717-720.
4. Block, B. A., Imagawa, T., Campbell, K. P. & Franzini-Armstrong, C. (1988) J. Cell Biol. 107, 2587-2600.
5. Arikkath, J. & Campbell, K. P. (2003) Curr. Opin. Neurobiol. 13, 298-307.
6. Preise, D., Held, B., Wissenbach, U., Pfeifer, A., Trost, C., Himmerkus, N., Schweig, U., Freichel, M., Bid, M., Hofmann, F., et al. (2000) J. Biol. Chem. 275, 14476-14481.
7. Obermair, G. J., Kugler, G., Baumgartner, S., Tuluc, P., Grabner, M. & Flucher, B. E. (2005) J. Biol. Chem. 280, 2229-2237.
8. Gregg, R. G., Messing, A., Strube, C., Beurg, M., Moss, R., Behan, M., Sukhareva, M., Haynes, S., Powell, J. A., Coronado, R., et al. (1996) Proc. Natl. Acad. Sci. USA 93, 13961-13966.
9. Tanabe, T., Beam, K. G., Powell, J. A. & Numa, S. (1988) Nature 336, 134-139.
10. Strube, C., Beurg, M., Powers, P. A., Gregg, R. G. & Coronado, R. (1996) Biophys. J. 71, 2531-2543.
11. Strube, C., Beurg, M., Sukhareva, M., Ahern, C. A., Powell, J. A., Powers, P. A., Gregg, R. G. & Coronado, R. (1998) Biophys. J. 75, 207-217.
12. Beurg, M., Sukhareva, M., Ahern, C. A., Conklin, M. W., Perez-Reyes, E., Powers, P. A., Gregg, R. G. & Coronado, R. (1999) Biophys. J. 76, 1744-1756.
13. Granato, M., van Eeden, F. J., Schach, U., Trowe, T., Brand, M., Furutani-Seiki, M., Haffter, F., Hammerschmidt, M., Heisenberg, C. P., Jiang, Y. J., et al. (1996) Development (Cambridge, U.K.) 123, 399-413.
14. Ono, F., Higashijima, S., Shcherbatko, A., Fetcho, J. R. & Brehm, P. (2001) J. Neurosci. 21, 5439-5448.
15. Flucher, B. E., Andrews, S. B. & Daniels, M. P. (1994) Mol. Biol. Cell 5, 1105-1118.
16. Weiss, R. G., O'Connell, K. M., Flucher, B. E., Allen, P. D., Grabner, M. & Dirksen, R. T. (2004) Am. J. Physiol. 287, C1094-C1102.
17. Adams, B. A., Tanabe, T., Mikami, A., Numa, S. & Beam, K. G. (1990) Nature 346, 569-572.
18. Cheung, A., Dantzig, J. A., Hollingworth, S., Baylor, S. M., Goldman, Y. E., Mitchison, T. J. & Straight, A. F. (2002) Nat. Cell Biol. 4, 83-88.
19. Grabner, M., Friedrich, K., Knaus, H. G., Striessnig, J., Scheffauer, F., Staudinger, R., Koch, W. J., Schwartz, A. & Glossmann, H. (1991) Proc. Natl. Acad. Sci. USA 88, 727-731.
20. Ruth, P., Rohrkasten, A., Biel, M., Bosse, E., Regulla, S., Meyer, H. E., Flockerzi, V. & Hofmann, F. (1989) Science 245, 1115-1118.
21. Morton, M. E. & Froehner, S. C. (1987) J. Biol. Chem. 262, 11904-11907.
22. Morton, M. E. & Froehner, S. C. (1989) Neuron 2, 1499-1506.
23. Pichler, M., Cassidy, T. N., Reimer, D., Haase, H., Kraus, R., Ostler, D. & Striessnig, J. (1997) J. Biol. Chem. 272, 13877-13882.
24. Glossmann, H. & Ferry, D. R. (1985) Methods Enzymol. 109, 513-550.
25. Takekura, H., Paolini, C., Franzini-Armstrong, C., Kugler, G., Grabner, M. & Flucher, B. E. (2004) Mol. Biol. Cell 15, 5408-5419.
26. Haffter, P., Granato, M., Brand, M., Mullins, M. C., Hammerschmidt, M., Kane, D. A., Odenthal, J., van Eeden, F. J., Jiang, Y. J., Heisenberg, C. P., et al. (1996) Development (Cambridge, U.K.) 123, 1-36.
27. Mendel, J. G. (1866) Verh. Nat. Vereins Brunn 4, 3-47.
28. Van Petegem, F., Clark, K. A., Chatelain, F. C. & Minor, D. L., Jr. (2004) Nature 429, 671-675.
29. Opatowsky, Y., Chen, C. C., Campbell, K. P. & Hirsch, J. A. (2004) Neuron 42, 387-399.
30. Sheridan, D. C., Cheng, W., Ahem, C. A., Mortenson, L., Alsammarae, D., Vallejo, P. & Coronado, R. (2003) Biophys. J. 84, 220-237.
31. Dolphin, A. C. (2003) J. Bioenerg. Biomembr. 35, 599-620.
32. Bichet, D., Cornet, V., Geib, S., Carlier, E., Volsen, S., Hoshi, T., Mori, Y. & De Waard, M. (2000) Neuron 25, 177-190.
33. Flucher, B. E., Phillips, J. L. & Powell, J. A. (1991) J. Cell Biol. 115, 1345-1356.
34. Protasi, F., Franzini-Armstrong, C. & Allen, P. D. (1998) J. Cell Biol. 140, 831-842.
35. Avila, G., O'Connell, K. M., Groom, L. A. & Dirksen, R. T. (2001) J. Biol. Chem. 276, 17732-17738.
36. Hoffman, R. & Gross, L. (1975) Nature 254, 586-588.