Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C

Science

Volumn 273, Issue 5272, 1996, Pages 248-251

  Shao, Xuguang ^a   Davletov, Bazbek A ^a,b   Sutton, R Bryan ^a   Südhof, Thomas C ^a   Rizo, Josep ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM BINDING PROTEIN; PROTEIN KINASE C; SYNAPTOTAGMIN; ASPARTIC ACID; MEMBRANE PROTEIN; NERVE PROTEIN; PHOSPHOLIPID; SYNAPTOTAGMIN I;

ARTICLE; BINDING AFFINITY; MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PH; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

ASPARTIC ACID; BASE SEQUENCE; CALCIUM; CALCIUM-BINDING PROTEINS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PHOSPHOLIPIDS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN KINASE C; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SYNAPTOTAGMIN I; SYNAPTOTAGMINS; TEMPERATURE;

EID: 0029666292     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5272.248     Document Type: Article

References (31)

1. N. C. J. Strynadka and M. N. G. James, Annu. Rev. Biochem. 58, 951 (1989).
2. Reviewed in Y. Nishizuka, Science 258, 607 (1992); A. Newton, Annu. Rev. Biophys. Biomol. Struct. 22, 1 (1993).
3. Reviewed in Y. Nishizuka, Science 258, 607 (1992); A. Newton, Annu. Rev. Biophys. Biomol. Struct. 22, 1 (1993).
4. N. Brose, K. Hofmann, Y. Hata, T. C. Südhof, J. Biol. Chem. 270, 25273 (1995).
5. N. Brose, A. G. Petrenko, T. C. Südhof, R. Jahn, Science 256, 1021 (1992); B. Ullrich et al., Neuron 13, 1281 (1994).
6. N. Brose, A. G. Petrenko, T. C. Südhof, R. Jahn, Science 256, 1021 (1992); B. Ullrich et al., Neuron 13, 1281 (1994).
7. J. D. Clark et al., Cell 65, 1043 (1991); T. Yamaguchi et al., J. Biol. Chem. 268, 27164 (1993).
8. J. D. Clark et al., Cell 65, 1043 (1991); T. Yamaguchi et al., J. Biol. Chem. 268, 27164 (1993).
9. C. Li et al., Nature 375, 594 (1995).
10. B. A. Davletov and T. C. Südhof, J. Biol. Chem. 268, 26386 (1993).
11. M. S. Perin, V. A. Fried, G. A. Mignery, R. Jahn, T. C. Südhof, Nature 345, 260 (1990); M. Geppert et al., Cell 79, 717 (1994); reviewed in T. C. Südhof, Nature 375, 645 (1995).
12. M. S. Perin, V. A. Fried, G. A. Mignery, R. Jahn, T. C. Südhof, Nature 345, 260 (1990); M. Geppert et al., Cell 79, 717 (1994); reviewed in T. C. Südhof, Nature 375, 645 (1995).
13. M. S. Perin, V. A. Fried, G. A. Mignery, R. Jahn, T. C. Südhof, Nature 345, 260 (1990); M. Geppert et al., Cell 79, 717 (1994); reviewed in T. C. Südhof, Nature 375, 645 (1995).
14. R. B. Sutton, B. A. Davletov, A. M. Berghuis, T. C. Südhof, S. R. Sprang, Cell 80, 929 (1995).
15. 15N NOESY-HMQC experiments [for original references see A. M. Gronenborn and G. M. Clore, Anal. Chem. 62, 2 (1990), and for experimental details see J. Rizo, Z.-P. Liu, L. M. Gierasch, J. Biomol. NMR 4, 741 (1994)].
16. 15N NOESY-HMQC experiments [for original references see A. M. Gronenborn and G. M. Clore, Anal. Chem. 62, 2 (1990), and for experimental details see J. Rizo, Z.-P. Liu, L. M. Gierasch, J. Biomol. NMR 4, 741 (1994)].
17. 2A domain at these two pHs.
18. X. Shao, B. A. Davletov, R. B. Sutton, T. C. Südhoff, J. Rizo, unpublished results.
19. 2+ into the crystals (9) are nearly identical (Cα root mean square deviation 0.2 Å), and the interproton distances predicted from them are similar (within 0.2 Å); differences larger than 0.5 Å are observed in very few cases.
20. 2+. These experiments were performed on an Aviv Model 62DS spectropolarimeter.
21. B. A. Davletov and T. C. Südhof, J. Biol. Chem. 269, 28547 (1994).
22. 2+ concentrations of 5, 20, 40, 80, 140, 250, 400, and 800 μM and 2 and 5 mM (21 hours per spectrum).
23. 2+ (9).
24. 2+ ion, the ion was repelled to infinity.
25. 2+ [R. Heidelberger, C. Heinemann, E. Neher, G. Mathews, Nature 371, 513 (1994)].
26. 2+ regulated [S. Sugita, Y. Hata, T. C. Südhof, J. Biol. Chem. 271, 1262 (1996)].
27. J.-H. Luo and I. B. Weinstein, J. Biol. Chem. 268, 23580 (1993).
28. 2+ with a Hill coefficient of 3.0 to 4.0.
29. 2+-induced shifts could be monitored throughout the titration.
30. Abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
31. We thank S. Sprang and C. Li for fruitful discussions and L. Kay for providing the sensitivity-enhanced HSQC pulse sequence. Supported by a joint grant from the William Randolph Hearst Foundation and the United Cerebral Palsy Research and Educational Foundation (J.R.), by a grant from the Welch Foundation (J.R.), and by NIH grants R29 NS33731-01A1 (J.R.) and RO1-MH52804-01 (T.C.S.).