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Identification of the Penta-EF-hand Protein ALG-2 as a Ca2+-dependent Interactor of Mucolipin-1

Vergarajauregui, Silvia, Martina, Jose A., Puertollano, Rosa·2009·Journal of Biological Chemistry
DOI 10.1074/jbc.m109.047241
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  • JIP4 phosphorylation following oxidative stress induces its interaction with the TRPML1/ALG2 complex, which also mediates dynein-dependent retrograde transport of lysosomes.

    “This may be explained by recent observations showing that JIP4 phosphorylation following oxidative stress induces its interaction with the TRPML1/ALG2 complex, which also mediates dynein-dependent retrograde transport of lysosomes9,38,39.”

    From TMEM55B links autophagy flux, lysosomal repair, and TFE3 activation in response to oxidative stress (2024) · cites this paper as [38]

    The Results report that mucolipin-1 (MCOLN1/TRPML1) interacts with ALG-2, supporting the named pairing. Our copy does not report JIP4 phosphorylation after oxidative stress, JIP4 binding to that pair, or dynein-dependent retrograde lysosome transport (searched: JIP4, oxidative stress, dynein-dependent transport). (LLM, conf=0.87)

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  • ALG-2 interacts with MCOLN1 in a calcium-dependent manner to recruit dynein-dynactin to lysosomes.

    “ALG-2 interacts with the lysosomal transient receptor potential channel MCOLN1 in a calcium-dependent manner to recruit dynein–dynactin to lysosomes28,29.”

    From TFEB regulates lysosomal positioning by modulating TMEM55B expression and JIP4 recruitment to lysosomes (2017) · cites this paper as [29]

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Research works printed but not linked: 79

  1. Bach, 2001, Mol. Genet. Metab., 73, 197, 10.1006/mgme.2001.3195 · DOI
  2. Amir, 1987, Pediatrics, 79, 953, 10.1542/peds.79.6.953 · DOI
  3. Altarescu, 2002, Neurology, 59, 306, 10.1212/WNL.59.3.306 · DOI
  4. Bach, 1975, Biochem. Biophys. Res. Commun., 66, 1483, 10.1016/0006-291X(75)90526-4 · DOI
  5. Tellez-Nagel, 1976, Arch. Neurol., 33, 828, 10.1001/archneur.1976.00500120032005 · DOI
  6. Bach, 1977, Am. J. Hum. Genet., 29, 610
  7. Crandall, 1982, Am. J. Med. Genet., 12, 301, 10.1002/ajmg.1320120308 · DOI
  8. Folkerth, 1995, J. Neuropathol. Exp. Neurol., 54, 154, 10.1097/00005072-199503000-00002 · DOI
  9. Chen, 1998, Proc. Natl. Acad. Sci. U.S.A., 95, 6373, 10.1073/pnas.95.11.6373 · DOI
  10. Slaugenhaupt, 1999, Am. J. Hum. Genet., 65, 773, 10.1086/302549 · DOI
  11. Bargal, 2000, Nat. Genet., 26, 118, 10.1038/79095 · DOI
  12. Bassi, 2000, Am. J. Hum. Genet., 67, 1110, 10.1016/S0002-9297(07)62941-3 · DOI
  13. Sun, 2000, Hum. Mol. Genet., 9, 2471, 10.1093/hmg/9.17.2471 · DOI
  14. Puertollano, 2009, Am. J. Physiol. Renal Physiol., 296, F1245, 10.1152/ajprenal.90522.2008 · DOI
  15. Pryor, 2006, Traffic, 7, 1388, 10.1111/j.1600-0854.2006.00475.x · DOI
  16. Vergarajauregui, 2006, Traffic, 7, 337, 10.1111/j.1600-0854.2006.00387.x · DOI
  17. Vergarajauregui, 2008, Biochem. J., 410, 417, 10.1042/BJ20070713 · DOI
  18. Kiselyov, 2005, J. Biol. Chem., 280, 43218, 10.1074/jbc.M508210200 · DOI
  19. LaPlante, 2004, Biochem. Biophys. Res. Commun., 322, 1384, 10.1016/j.bbrc.2004.08.045 · DOI
  20. Cantiello, 2005, Pfluegers Arch., 451, 304, 10.1007/s00424-005-1448-9 · DOI
  21. Soyombo, 2006, J. Biol. Chem., 281, 7294, 10.1074/jbc.M508211200 · DOI
  22. Dong, 2008, Nature, 455, 992, 10.1038/nature07311 · DOI
  23. Piper, 2004, Trends Cell Biol., 14, 471, 10.1016/j.tcb.2004.07.010 · DOI
  24. Treusch, 2004, Proc. Natl. Acad. Sci. U.S.A., 101, 4483, 10.1073/pnas.0400709101 · DOI
  25. LaPlante, 2006, Mol. Genet. Metab., 89, 339, 10.1016/j.ymgme.2006.05.016 · DOI
  26. Vergarajauregui, 2008, Hum. Mol. Genet., 17, 2723, 10.1093/hmg/ddn174 · DOI
  27. Venkatachalam, 2008, Cell, 135, 838, 10.1016/j.cell.2008.09.041 · DOI
  28. Vergarajauregui, 2008, Autophagy, 4, 832, 10.4161/auto.6567 · DOI
  29. Miedel, 2008, J. Exp. Med., 205, 1477, 10.1084/jem.20072194 · DOI
  30. Venugopal, 2009, J. Cell. Physiol., 219, 344, 10.1002/jcp.21676 · DOI
  31. Luzio, 2007, Biochem. Soc. Trans., 35, 1088, 10.1042/BST0351088 · DOI
  32. Rodríguez, 1997, J. Cell Biol., 137, 93, 10.1083/jcb.137.1.93 · DOI
  33. Gordon, 1993, J. Biol. Chem., 268, 26107, 10.1016/S0021-9258(19)74287-2 · DOI
  34. LaPlante, 2002, FEBS Lett., 532, 183, 10.1016/S0014-5793(02)03670-0 · DOI
  35. Xu, 2007, Proc. Natl. Acad. Sci. U.S.A., 104, 18321, 10.1073/pnas.0709096104 · DOI
  36. Grimm, 2007, Proc. Natl. Acad. Sci. U.S.A., 104, 19583, 10.1073/pnas.0709846104 · DOI
  37. Lo, 1999, Biochemistry, 38, 7498, 10.1021/bi990034n · DOI
  38. Maki, 2002, Biochim. Biophys. Acta, 1600, 51, 10.1016/S1570-9639(02)00444-2 · DOI
  39. Tarabykina, 2004, Front. Biosci., 9, 1817, 10.2741/1358 · DOI
  40. Missotten, 1999, Cell Death Differ., 6, 124, 10.1038/sj.cdd.4400456 · DOI
  41. Vito, 1999, J. Biol. Chem., 274, 1533, 10.1074/jbc.274.3.1533 · DOI
  42. Katoh, 2005, Biochem. J., 391, 677, 10.1042/BJ20050398 · DOI
  43. Yamasaki, 2006, Mol. Biol. Cell, 17, 4876, 10.1091/mbc.e06-05-0444 · DOI
  44. la Cour, 2007, Biochem. Biophys. Res. Commun., 353, 1063, 10.1016/j.bbrc.2006.12.143 · DOI
  45. Shibata, 2007, Biochem. Biophys. Res. Commun., 353, 756, 10.1016/j.bbrc.2006.12.101 · DOI
  46. Mahul-Mellier, 2006, J. Neurosci., 26, 542, 10.1523/JNEUROSCI.3069-05.2006 · DOI
  47. Rao, 2004, J. Biol. Chem., 279, 177, 10.1074/jbc.M304490200 · DOI
  48. la Cour, 2003, Am. J. Pathol., 163, 81, 10.1016/S0002-9440(10)63632-2 · DOI
  49. Wang, 2006, J. Proteome Res., 5, 1214, 10.1021/pr050406g · DOI
  50. Hoffert, 2007, J. Proteome Res., 6, 3501, 10.1021/pr0701153 · DOI
  51. Fath, 2007, Cell, 129, 1325, 10.1016/j.cell.2007.05.036 · DOI
  52. Satoh, 2002, Biochem. Biophys. Res. Commun., 291, 1166, 10.1006/bbrc.2002.6600 · DOI
  53. Satoh, 2002, Biochim. Biophys. Acta, 1600, 61, 10.1016/S1570-9639(02)00445-4 · DOI
  54. Tarabykina, 2000, J. Biol. Chem., 275, 10514, 10.1074/jbc.275.14.10514 · DOI
  55. Shibata, 2008, J. Biol. Chem., 283, 9623, 10.1074/jbc.M800717200 · DOI
  56. Shibata, 2004, J. Biochem., 135, 117, 10.1093/jb/mvh014 · DOI
  57. Trioulier, 2004, J. Biol. Chem., 279, 2046, 10.1074/jbc.M309243200 · DOI
  58. Chen, 2005, Biochem. Biophys. Res. Commun., 333, 51, 10.1016/j.bbrc.2005.05.074 · DOI
  59. Hwang, 2002, FEBS Lett., 529, 183, 10.1016/S0014-5793(02)03329-X · DOI
  60. Babst, 1998, EMBO J., 17, 2982, 10.1093/emboj/17.11.2982 · DOI
  61. Fujita, 2003, J. Cell Sci., 116, 401, 10.1242/jcs.00213 · DOI
  62. Dunn, 1996, Exp. Eye Res., 62, 155, 10.1006/exer.1996.0020 · DOI
  63. Aukunuru, 2001, Pharm. Res., 18, 565, 10.1023/A:1011060705599 · DOI
  64. Miedel, 2006, J. Biol. Chem., 281, 12751, 10.1074/jbc.M511104200 · DOI
  65. Christensen, 2002, J. Cell Sci., 115, 599, 10.1242/jcs.115.3.599 · DOI
  66. Draeby, 2007, Arch. Biochem. Biophys., 467, 87, 10.1016/j.abb.2007.07.028 · DOI
  67. Suzuki, 2008, Structure, 16, 1562, 10.1016/j.str.2008.07.012 · DOI
  68. Suzuki, 2009, Biochem. Soc. Trans., 37, 190, 10.1042/BST0370190 · DOI
  69. Yap, 2000, J. Struct. Funct. Genomics, 1, 8, 10.1023/A:1011320027914 · DOI
  70. Okumura, 2009, Biochem. Biophys. Res. Commun., 386, 237, 10.1016/j.bbrc.2009.06.015 · DOI
  71. Bach, 2005, Pflugers Arch, 451, 313, 10.1007/s00424-004-1361-7 · DOI
  72. Fares, 2001, Nat. Genet., 28, 64
  73. Manzoni, 2004, FEBS Lett., 567, 219, 10.1016/j.febslet.2004.04.080 · DOI
  74. Thompson, 2007, BMC Cell Biol., 8, 54, 10.1186/1471-2121-8-54 · DOI
  75. Holroyd, 1999, Mol. Biol. Cell, 10, 3035, 10.1091/mbc.10.9.3035 · DOI
  76. Yan, 2004, J. Biol. Chem., 279, 18270, 10.1074/jbc.M400093200 · DOI
  77. Martín-Nieto, 1998, Biochemistry, 37, 227, 10.1021/bi971765v · DOI
  78. Tebar, 2002, Mol. Biol. Cell, 13, 2057, 10.1091/mbc.01-12-0571 · DOI
  79. Raychowdhury, 2004, Hum. Mol. Genet., 13, 617, 10.1093/hmg/ddh067 · DOI

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Metadata

Authors
Vergarajauregui, S., Martina, J. A., & Puertollano, R.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2009-12
Volume
284
Issue
52
Pages
36357-36366
ISSN
0021-9258
DOI
10.1074/jbc.m109.047241
Cited by
85
References
1
Language
en
Licence

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