Membrane phosphatidylserine regulates surface charge and protein localization

Science

Volumn 319, Issue 5860, 2008, Pages 210-213

  Yeung, Tony ^a   Gilbert, Gary E ^b   Shi, Jialan ^b   Silvius, John ^c   Kapus, Andras ^d   Grinstein, Sergio ^a  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b BRIGHAM AND WOMEN S HOSPITAL   (United States)

^c MCGILL UNIVERSITY   (Canada)

^d ST MICHAEL'S HOSPITAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ANION; PHOSPHATIDYLSERINE; PHOSPHOLIPID;

AMINO ACID; CALCIUM; CYTOLOGY; MEMBRANE; PROTEIN;

ARTICLE; BIOSENSOR; CALCIUM TRANSPORT; CELL MEMBRANE; CELLULAR DISTRIBUTION; CYTOSOL; ELECTRICITY; ENDOCYTOSIS; ENDOSOME; LYSOSOME; MEMBRANE TRANSPORT; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN TARGETING; REGULATORY MECHANISM; SURFACE CHARGE; SURFACE PROPERTY;

ANIMALS; BIOSENSING TECHNIQUES; CELL LINE; CELL MEMBRANE; ELECTROSTATICS; ENDOCYTOSIS; ENDOSOMES; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; HYDROPHOBICITY; INTRACELLULAR MEMBRANES; LYSOSOMES; MICROSCOPY, CONFOCAL; MILK PROTEINS; ORGANELLES; PHOSPHATIDYLSERINES; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION; SURFACE PROPERTIES;

EID: 38149094836     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1152066     Document Type: Article

References (20)

1. S. McLaughlin, D. Murray, Nature 438, 605 (2005).
2. W. D. Heo et al., Science 314, 1458 (2006).
3. J. E. Vance, R. Steenbergen, Prog. Lipid Res. 44, 207 (2005).
4. M. H. Andersen, H. Graversen, S. N. Fedosov, T. E. Petersen, J. T. Rasmussen, Biochemistry 39, 6200 (2000).
5. J. Shi, C. W. Heegaard, J. T. Rasmussen, G. E. Gilbert, Biochim. Biophys. Acta 1667, 82 (2004).
6. Materials and methods are available as supporting material on Science Online.
7. G. E. Gilbert, B. C. Furie, B. Furie, J. Biol. Chem. 265, 815 (1990).
8. K. Atkinson, S. Fogel, S. A. Henry, J. Biol. Chem. 255, 6653 (1980).
9. G. E. Gilbert, R. J. Kaufman, A. A. Arena, H. Miao, S. W. Pipe, J. Biol. Chem. 277, 6374 (2002).
10. T. Yeung et al., Science 313, 347 (2006).
11. M. O. Roy, R. Leventis, J. R. Silvius, Biochemistry 39, 8298 (2000).
12. R. Leventis, J. R. Silvius, Biochemistry 37, 7640 (1998).
13. D. Murray et al., Biochemistry 37, 2145 (1998).
14. M. Miaczynska, L. Pelkmans, M. Zerial, Curr. Opin. Cell Biol. 16, 400 (2004).
15. Single-letter abbreviations for the amino acid residues used in this report are as follows: A, Ala; D, Asp; E, Glu; K, Lys; L, Leu; Q, Gln; and R, Arg.
16. J. F. Hancock, H. Paterson, C. J. Marshall, Cell 63, 133 (1990).
17. K. Balasubramanian, B. Mirnikjoo, A. J. Schroit, J. Biol. Chem. 282, 18357 (2007).
18. T. G. Bivona et al., Mol. Cell 21, 481 (2006).
19. S. McLaughlin, A. Aderem, Trends Biochem. Sci. 20, 272 (1995).
20. We thank V. A. Novakovic for excellent technical assistance. Supported by the Heart and Stroke Foundation of Canada, Canadian Institutes of Health Research, and NIH. S.G. holds the Pitblado Chair in Cell Biology.