Complexin controls the force transfer from SNARE complexes to membranes in fusion

Science

Volumn 323, Issue 5913, 2009, Pages 516-521

  Maximov, Anton ^a,d   Tang, Jiong ^a,b   Yang, Xiaofei ^a,b   Pang, Zhiping P ^a,b   Südhof, Thomas C ^a,b,c  

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

^b STANFORD UNIVERSITY   (United States)

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

^d SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; COMPLEXIN; MEMBRANE FUSION PROTEIN; MUTANT PROTEIN; N ETHYLMALEIMIDE SENSITIVE FACTOR; PROTEIN; SNARE PROTEIN; SYNAPTOBREVIN; UNCLASSIFIED DRUG;

CATALYSIS; MEMBRANE; MUTATION; PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BRAIN CELL; CELL MEMBRANE TRANSPORT; COMPLEX FORMATION; CONTROLLED STUDY; EXCITATORY POSTSYNAPTIC POTENTIAL; FORCE; GENE INSERTION SEQUENCE; LOSS OF FUNCTION MUTATION; MEMBRANE FUSION; MOLECULAR DYNAMICS; MOUSE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; RAT; RNA INTERFERENCE; SYNAPSE VESICLE; TRANSPORT KINETICS;

ACTION POTENTIALS; AMINO ACID SEQUENCE; ANIMALS; CALCIUM; CELLS, CULTURED; EXCITATORY POSTSYNAPTIC POTENTIALS; MEMBRANE FUSION; MICE; MICE, KNOCKOUT; MUTANT PROTEINS; NERVE TISSUE PROTEINS; NEURONS; PROTEIN BINDING; R-SNARE PROTEINS; SNARE PROTEINS; SYNAPSES; SYNAPTIC VESICLES; SYNAPTOTAGMINS;

EID: 58849164361     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1166505     Document Type: Article

References (25)

1. J. B. Sørensen, Trends Neurosci. 28, 453 (2005).
2. R. Jahn, R. H. Scheller, Nat. Rev. Mol. Cell Biol. 7, 631 (2006).
3. M. Verhage, R. F. Toonen, Curr. Opin. Cell Biol. 19, 402 (2007).
4. M. Geppert et al., Cell 79, 717 (1994).
5. R. Fernandez-Chacon et al., Nature 410, 41 (2001).
6. M. Yoshihara, J. T. Littleton, Neuron 36, 897 (2002).
7. K. Reim et al., Cell 104, 71 (2001).
8. X. Chen et al., Neuron 33, 397 (2002).
9. A. Bracher, J. Kadlec, H. Betz, W. Weissenhorn, J. Biol. Chem. 277, 26517 (2002).
10. M. Xue et al., Nat. Struct. Mol. Biol. 14, 949 (2007).
11. C. G. Giraudo, W. S. Eng, T. J. Melia, J. E. Rothman, Science 313, 676 (2006), published online 22 June 2006; 10.1126/science.1129450.
12. C. G. Giraudo et al., J. Biol. Chem. 283, 21211 (2008).
13. J. R. Schaub, X. Lu, B. Doneske, Y. K. Shin, J. A. McNew, Nat. Struct. Mol. Biol. 13, 748 (2006).
14. T. Y. Yoon et al., Nat. Struct. Mol. Biol. 15, 707 (2008).
15. S. Huntwork, J. T. Littleton, Nat. Neurosci. 10, 1235 (2007).
16. K. Weninger, M. E. Bowen, U. B. Choi, S. Chu, A. T. Brunger, Structure 16, 308 (2008).
17. R. Guan, H. Dai, J. Rizo, Biochemistry 47, 1474 (2008).
18. S. Schoch et al., Science 294, 1117 (2001).
19. Single-letter 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.
20. For a description of the experimental procedures, see the supporting online material.
21. J. Tang et al., Cell 126, 1175 (2006).
22. A. Maximov, T. C. Sûdhof, Neuron 48, 547 (2005).
23. K. Hu, J. Carroll, C. Rickman, B. Davletov, J. Biol. Chem. 277, 41652 (2002).
24. C. G. Giraudo et al., Science 323, 512 (2009).
25. We thank J. Rizo and L. Chen for advice and critical comments. This study was supported by an investigatorship to T.C.S. from the Howard Hughes Medical Institute.