Localization and processing of CLN3, the protein associated to batten disease: Where is it and what does it do?

Journal of Neuroscience Research

Volumn 59, Issue 1, 2000, Pages 19-23

  Pearce, David A ^a  

^a UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY   (United States)

Author keywords

Batten disease; CLN3; Lysosome endosome; Protein trafficking

Indexed keywords

MEMBRANE PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ENDOPLASMIC RETICULUM; ENDOSOME; GOLGI COMPLEX; HUMAN; INTRACELLULAR TRANSPORT; LYSOSOME; NEURONAL CEROID LIPOFUSCINOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN TARGETING; SHORT SURVEY;

ANIMALS; CYCLINS; HUMANS; MEMBRANE GLYCOPROTEINS; MOLECULAR CHAPERONES; NEURONAL CEROID-LIPOFUSCINOSES; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0033963467     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4547(20000101)59:1<19::AID-JNR3>3.0.CO;2-Y     Document Type: Short Survey

References (41)

1. Cameron PL, Sudhof TC, Jahn R, De Camilli P. 1991. Colocalization of synaptophysin with transferrin receptors: implications for synaptic vesicle biogeneisis. J. Cell Biol 115:151-154.
2. Casey PJ, Seabra MC. 1996. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 271:5289-5292.
3. Choy E, Chiu VK, Silletti J, Feoktistov M, Morimoto T, Michaelson D, Ivanov IE, Philips MR. 1999. Endomembrane trafficking of Ras: the CAAX motif targets proteins to the ER and golgi. Cell 98:69-80.
4. Croopnick JB, Choi HC, Mueller DM. 1998. The subcellular location of the yeast Saccharomyces cerevisiae homologue of the protein defective in juvenile form of Batten disease. Biochem Biophys Res Comm 250:335-341.
5. Ezaki J, Wolfe LS, Higuit T, Ishidoh K, Kominami E. 1995a. Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten disease). J Neurochem 64:733-741.
6. Ezaki J, Wolfe LS, Ishidoh K, Kominami E. 1995b. Abnormal degradative pathway of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofusinosis (Batten disease). Am J Med Genet 57:254-259.
7. Golabek AA, Kaczmarski W, Kida E, Kaczmarski A, Michalewski M, Wisniewski KE. 1999. Expression studies of CLN3 protein (Battenin) in fusion with the green fluorescent protein in mammalian cells in vitro. Mol Genet Metab 66:277-282.
8. Hall NA, Lake BD, Dewji NN, Patrick ND. 1991. Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease. Biochem J 275:269-272.
9. Haltia M, Rapola L, Santavuori P, Keranen A. 1973. Infantile type of so-called neuronal ceroid lipofuscinosis. 2. J Neurol Sci 18:269-285.
10. Haskell RE, Derksen TA, Davidson BL. 1999. Intracellular trafficking of the JNCL protein CLN3. Mol Genet Metabol 66:253-260.
11. Haucke V, De Camilli P. 1999. AP-2 recruitment to synaptotagmin stimulated by tyrosine-based endocytic motifs. Science 285:1268-1271.
12. International Batten Disease Consortium. 1995. Isolation of a novel gene underlying Batten disease. Cell 82:949-957.
13. Janes RW, Munroe PB, Mitchison HM, Gardiner RM, Mole SE, Wallace BA. 1996. A model for Batten disease protein CLN3: functional implications from homology and mutations. FEBS Lett 399:75-77.
14. Jarvela I, Sainio M Rantamaki, T, Olkkonen VM, Carpen O, Peltonen L, Jalanko A. 1998. Biosynthesis and intracellular targeting of the CLN3 protein defective in Batten disease. Hum Mol Genet 7:85-90.
15. Jarvela I, Lehtovirta M, Tikknen R, Kyttala A, Jalenko A. 1999. Defective intracellular transport of CLN3 is the molecular basis of Batten disease (JNCL). Hum Mol Genet 8: 1091-1098.
16. Kaczmarski W, Kida E, Lach A, Rubenstein R, Zhong N, Wisniewski KE. 1997. Expression studies of CLN3 protein. Neuropediatrrics 28:33-36.
17. Kaczmarski W, Wisniewski KE, Golabek A, Kaczmarski A, Kida E, Michalewski M. 1999. Studies of membrane association of CLN3 protein. Mol Genet Metabol 66:261-264.
18. Katz ML, Gao C-L, Prabhakaram M, Shibuya H, LiuP-O, Johnson GS. 1997. Immunochemical localization of the Batten disease (CLN3) protein in retina. Invest Opthalmol Vis Sci 38:3375-2386.
19. Kida E, Kaczmarski W, Golabek AA, Kaczmarski A, Michalewski M, Wisniewski KE. 1999. Analysis of intracellular distribution and trafficking of the CLN3 protein in fusion with the green fluorescent protein in vitro. Mol Genet Metabol 66:265-271.
20. Koenig H, McDonald T, Nellhaus G. 1964. Morphological and histochemical studies of neurolipidosis by light and electron microscopy. I Neuropathol Exp Neurol 23:191-193.
21. Kominami E, Ezaki J, Muno D, Ishido K, Ueno T, Wolfe LS. 1992. Specific storage of subunit c of mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease). J Biochem 111:278-282.
22. Kramer H, Phistry M. 1996. Mutations in the Drosophila hook gene inhibit endocytosis of the boss transmembrane ligand into multivesicular bodies. J Cell Biol 133: 1205-1215.
23. Kramer H, Phistry M. 1999. Genetic analysis of hook, a gene required for endocytic trafficking in Drosophila. Genetics 151:675-684.
24. Kremmidiotis G, Lensink IL, Bilton RL, Woollatt E, Chataway TK, Sutherland GR, Callen DF. 1999. The Batten disease gene product (CLN3p) is a golgi integral membrane protein. Hum Mol Genet 8:523-531.
25. Margraf LR, Boriack RL, Routheut AAJ, Cuppen I Alhilali L, Bennett CJ, Bennett MJ. 1999. Tissue expression and subcellular localization of CLN3, the Batten disease protein. Mol Genet Metabol 66:283-289.
26. McGeoch JE, Guidotti G. 1997. A 0.1-700 Hz current through a voltage-clamped pore: candidate protein for initiator of neural oscillations. Brain Res 766:188-194.
27. McGeoch JE, Palmer DN. 1999. Ion pores made of mitochondrial ATP synthase subunit c in the neuronal plasma membrane and Batten disease. Mol Genet Metabol 66:387-392.
28. Michalewski MP, Kaczmarski W, Golabek AA, Kida E, Kaczmarski A, Wisniewski KE. 1999. Posttranslational modification of CLN3 protein and its possible functional implication. Mol Genet Metabol 66:272-276.
29. Mole SE. 1998. Batten disease: four genes and still counting. Neurobiol Disease 5:287-303.
30. Moser TL, Stack MS, Asplin I, Enghild JJ, Hojrup P, Everitt L, Hubchak S, Schraper HW, Pizzo SV. 1999. Angiostatin binds ATP synthase on the surface of human endothelial cells. Proc Natl Acad Sci USA 96:2811-2816.
31. Ohno H, Stewart J, Fournier MC, Bosshart H, Rhee I, Miyatake S, Saito T, Gallusser A Kirchhausen T, Bonifacino JS. 1995. Interaction of tyrosine-based sorting signals with clathrin-associated proteins. Science 269:1872-1875.
32. Palmer DN, Fearnley IM, Walker JE, Hall NE, Lake BD, Wolfe LS, Haltia M, Martinus RD, Jolly RD. 1992. Mitochondrial ATP synthase subunit c storage in the ceroid-liporuscinoses Batten disease. Am J Med Genet 42:561-567.
33. Palmer DN, Bayliss SL, Westlake VJ. 1995. Batten disease and the ATP synthase subunit c turnover pathway: raising antibodies to subunit c. Am J Med Genet 57:260-265.
34. Pearce DA, Sherman F. 1997. BTN1, a yeast gene corresponding to the human gene responsible for Batten's disease, is not essential for viability, mitochondrial function, or degradation of mitochondrial ATP synthase. Yeast 13:691-697.
35. Pearce DA, Sherman F. 1998. A yeast model for the study of Batten disease. Proc Natl Acad Sci USA 95:6915-6918.
36. Pearce DA, Sherman F 1999. Investigation of Batten disease with the yeast Saccharomyces cerevisiae. Mol Genet Metabol 66:314-319.
37. Pearce DA, Ferea T, Nosel SA, Das B, Sherman F. 1999. Action of Btn1p, the yeast orthologue of the gene mutated in Batten disease. Nat Genet 22:55-58.
38. +-ATPase. Cell Stress Chaper 2:12-24.
39. Pullarkat RK, Morris GN. 1997. Farnesylation of Batten disease CLN3 protein. Neuropediatrics 28:42-44.
40. Reiss Y, Goldstein JL, Seabra MC, Casey PJ, Brown MS. 1990. Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides. Cell 62:81-88.
41. Sunio A, Metcalf AB, Kramer H. 1999. Genetic dissection of endocytic trafficking in Drosophila using a horseradish peroxidase-bride of sevenless chimera: hook is required for normal maturation of multivesicular endosomes. Mol Biol Cell 10:847-859.