TRP-ML1 regulates lysosomal pH and acidic lysosomal lipid hydrolytic activity

Journal of Biological Chemistry

Volumn 281, Issue 11, 2006, Pages 7294-7301

  Soyombo, Abigail A ^a   Tjon Kon Sang, Sandra ^a   Rbaibi, Youssef ^b   Bashllari, Enkelejda ^b   Bisceglia, Jill ^b   Muallem, Shmuel ^a   Kiselyov, Kirill ^a,b  

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

^b UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDITY; BIOLOGICAL MEMBRANES; DISEASES; LIPIDS; PATHOLOGY; PH;

LYSOSOMES; MUCOLIPIDOSIS; ORGANELLES;

MUTAGENESIS;

CALCIUM; CHLOROQUINE; HYDROLASE; ION CHANNEL; LIPID; NIGERICIN; PROTEIN TRP ML1; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; ACRIDINE ORANGE; CARBOXYLIC ACID; CHOLESTEROL ESTERASE; IONOPHORE; LIPA PROTEIN, HUMAN; MAGNESIUM; MCOLN1 PROTEIN, HUMAN; OREGON GREEN 488 CARBOXYLIC ACID; PROTON; TRANSIENT RECEPTOR POTENTIAL CHANNEL M;

ARTICLE; CELL FRACTIONATION; CELL ORGANELLE; DRUG ACTIVITY; GENE CONTROL; GENE MUTATION; HUMAN; LIPID HYDROLYSIS; LIPOLYSIS; LYSOSOME; MEMBRANE FUSION; METABOLIC DISORDER; PH; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN METABOLISM; PROTEIN SYNTHESIS; BIOLOGICAL MODEL; CALCIUM SIGNALING; CELL LINE; CELL MEMBRANE; CHEMISTRY; ELECTRON MICROSCOPY; FLUORESCENCE MICROSCOPY; HYDROLYSIS; LYSOSOME STORAGE DISEASE; METABOLISM; MUTATION; THIN LAYER CHROMATOGRAPHY;

ACRIDINE ORANGE; CALCIUM; CALCIUM SIGNALING; CARBOXYLIC ACIDS; CELL LINE; CELL MEMBRANE; CHLOROQUINE; CHOLESTEROL ESTERASE; CHROMATOGRAPHY, THIN LAYER; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLASES; HYDROLYSIS; IONOPHORES; LIPASE; LIPIDS; LYSOSOMAL STORAGE DISEASES; LYSOSOMES; MAGNESIUM; MEMBRANE FUSION; MICROSCOPY, ELECTRON; MICROSCOPY, FLUORESCENCE; MODELS, BIOLOGICAL; MUTATION; PHENOTYPE; PROTONS; SUBCELLULAR FRACTIONS; TRPM CATION CHANNELS;

EID: 33646344988     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M508211200     Document Type: Article

References (40)

1. Bach, G. (2001) Mol. Genet. Metab. 73, 197-203
2. Slaugenhaupt, S. A. (2002) Curr. Mol. Med. 2, 445-450
3. Fares, H., and Greenwald, I. (2001) Nat. Genet. 28, 64-68
4. Bach, G., and Desnick, R. J. (1988) Enzyme 40, 40-44
5. Bargal, R., and Bach, G. (1997) J. Inherit. Metab. Dis. 20, 625-632
6. Chen, C. S., Bach, G., and Pagano, R. E. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 6373-6378
7. LaPlante, J. M., Ye, C. P., Quinn, S. J., Goldin, E., Brown, E. M., Slaugenhaupt, S. A., and Vassilev, P. M. (2004) Biochem. Biophys. Res. Commun. 322, 1384-1391
8. Manzoni, M., Monti, E., Bresciani, R., Bozzato, A., Barlati, S., Bassi, M. T., and Borsani, G. (2004) FEBS Lett. 567, 219-224
9. Treusch, S., Knuth, S., Slaugenhaupt, S. A., Goldin, E., Grant, B. D., and Fares, H. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 4483-4488
10. Kiselyov, K., Chen, J., Rbaibi, Y., Oberdick, D., Tjon-Kon-Sang, S., Shcheynikov, N., Muallem, S., and Soyombo, A. (2005) J. Biol. Chem. 280, 43218-43223
11. LaPlante, J. M., Falardeau, J., Sun, M., Kanazirska, M., Brown, E. M., Slaugenhaupt, S. A., and Vassilev, P. M. (2002) FEBS Lett. 532, 183-187
12. Bach, G. (2004) Pfluegers Arch. Eur. J. Physiol. 451, 313-317
13. Raychowdhury, M. K., Gonzalez-Perrett, S., Montalbetti, N., Timpanaro, G. A., Chasan, B., Goldmann, W. H., Stahl, S., Cooney, A., Goldin, E., and Cantiello, H. F. (2004) Hum. Mol. Genet. 13, 617-627
14. Mullins, C., and Bonifacino, J. S. (2001) BioEssays 23, 333-343
15. Luzio, J. P., Poupon, V., Lindsay, M. R., Mullock, B. M., Piper, R. C., and Pryor, P. R. (2003) Mol. Membr. Biol. 20, 141-154
16. Luzio, J. P., Pryor, P. R., Gray, S. R., Gratian, M. J., Piper, R. C., and Bright, N. A. (2005) Biochem. Soc. Symp. 72, 77-86
17. Piper, R. C., and Luzio, J. P. (2004) Trends Cell Biol. 14, 471-473
18. Bassi, M. T., Manzoni, M., Monti, E., Pizzo, M. T., Ballabio, A., and Borsani, G. (2000) Am. J. Hum. Genet. 67, 1110-1120
19. Duncan, J. A., and Gilman, A. G. (1996) J. Biol. Chem. 271, 23594-23600
20. Burton, B. K., Emery, D., and Mueller, H. W. (1980) Clin. Chim. Acta 101, 25-32
21. Berge, R. K., and Farstad, M. (1979) Eur. J. Biochem. 96, 393-401
22. Yuan, J. P., Kiselyov, K., Shin, D. M., Chen, J., Shcheynikov, N., Kang, S. H., Dehoff, M. H., Schwarz, M. K., Seeburg, P. H., Muallem, S., and Worley, P. F. (2003) Cell 114, 777-789
23. Srinivas, S. P., Ong, A., Goon, L., and Bonanno, J. A. (2002) Investig. Ophthalmol. Vis. Sci. 43, 2341-2350
24. Haller, T., Dietl, P., Deetjen, P., and Volkl, H. (1996) Cell Calcium 19, 157-165
25. Pillay, C. S., Elliott, E., and Dennison, C. (2002) Biochem. J. 363, 417-429
26. Kim, J. J., and Dahms, N. M. (2001) Results Probl. Cell Differ. 33, 39-56
27. Lake, J. R., Van Dyke, R. W., and Scharschmidt, B. F. (1987) Gastroenterology 92, 1251-1261
28. Bach, G., Chen, C. S., and Pagano, R. E. (1999) Clin. Chim. Acta 280, 173-179
29. Decoursey, T. E. (2003) Physiol. Rev. 83, 475-579
30. Morgan, D., and DeCoursey, T. E. (2003) Front. Biosci. 8, 1266-1279
31. DeCoursey, T. E. (1991) Biophys. J. 60, 1243-1253
32. DeCoursey, T. E., and Cherny, V. V. (1996) Biophys. J. 71, 182-193
33. DeCoursey, T. E. (1998) Front. Biosci. 3, 477-482
34. Bach, G., Zeigler, M., Schaap, T., and Kohn, G. (1979) Biochem. Biophys. Res. Commun. 90, 1341-1347
35. Bargal, R., and Bach, G. (1989) Clin. Chim. Acta 181, 167-174
36. Zeigler, M., Bargal, R., Suri, V., Meidan, B., and Bach, G. (1992) Prenat. Diagn. 12, 1037-1042
37. Goldin, E., Cooney, A., Kaneski, C. R., Brady, R. O., and Schiffmann, R. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 8562-8566
38. Tzagoloff, A., Barrientos, A., Neupert, W., and Herrmann, J. M. (2004) J. Biol. Chem. 279, 19775-19780
39. Ostrowska, H., Krukowska, K., Kalinowska, J., Orlowska, M., and Lengiewicz, I. (2003) Cell. Mol. Biol. Lett. 8, 19-24
40. Pshezhetsky, A. V., and Ashmarina, M. (2001) Prog. Nucleic Acid Res. Mol. Biol. 69, 81-114