Posttranslational modification of CLN3 protein and its possible functional implication

Molecular Genetics and Metabolism

Volumn 66, Issue 4, 1999, Pages 272-276

  Michalewski, Martin P ^a   Kaczmarski, Wojciech ^a   Golabek, Adam A ^b   Kida, Elizabeth ^b   Kaczmarski, Aleksandra ^a   Wisniewski, Krystyna E ^c  

^a NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

^b MOSSAKOWSKI MEDICAL RESEARCH CENTRE   (Poland)

^c SUNY DOWNSTATE MEDICAL CENTER   (United States)

Author keywords

Batten disease; CLN3; GFP; Phosphorylation

Indexed keywords

CEROID; GREEN FLUORESCENT PROTEIN; LIPOFUSCIN; PHOSPHATASE; PROTEIN KINASE;

AMINO ACID ANALYSIS; ANIMAL CELL; CONFERENCE PAPER; GENETIC CODE; HUMAN; NEURONAL CEROID LIPOFUSCINOSIS; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN PROCESSING;

EID: 0032806925     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1006/mgme.1999.2818     Document Type: Conference Paper

References (16)

1. Goebel H. The neuronal ceroid-lipofuscinosis. J Child Neurol. 10:1995;424-437.
2. Cell. 82:1995;948-957.
3. Munroe P B, Mitchison H M, O'Rawe A M, Anderson J W, Boustany R-M, Lerner T J, Taschner P EM, de Vos N, Breuning M H, Gardiner R M, Mole S E. Spectrum of mutations in the Batten disease gene. Am J Hum Genet. 61:1997;310-316.
4. Jarvela I, Sainio M, Rantamaki T, Olkkonen V M, Carpen O, Peltonen L, Jalanko A. Biosynthesis and intracellular targeting of the CLN3 protein defective in Batten disease. Hum MolGenet. 7:1998;85-90.
5. Golabek, A, A, Kaczmarski, W, Kida, E, Kaczmarski, A, Michalewski, M, P, Connel, F, Wisniewski, K, E, Wild type CLN3 protein (battenin), but not its mutant associated with classical juvenile neuronal ceroid lipofuscinosis, is a integral membrane protein of lysosomal compartments.
6. Kaczmarski W, Kida E, Lach A, Rubenstein R, Zhong N, Wisniewski K E. Expression studies of CLN3 protein. Neuropediatrics. 28:1997;33-36.
7. Janes R W, Munroe P B, Mitchison H M, Gardiner R M, Mole S E, Wallace B A. A model for Batten disease protein CLN3: Functional implication from homology and mutations. FEBS Lett. 399:1996;75-77.
8. Michalewski M P, Kaczmarski W, Golobek A A, Kida E, Kaczmarski A, Wisniewski K E. Evidence for phosphorylation of CLN3 protein associated with Batten disease. Biochem Biophys Res Commun. 253:1998;458-462.
9. Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets:procedure and some applications. Proc Natl Acad Sci USA. 76:1979;4350-4359.
10. Valenzano K J, Kallay L M, Lobel P. An assay to detect glycoproteins that contain mannose 6-phosphate. Anal Biochem. 209:1993;156-162.
11. Bylund D B, Huang T-S. Decomposition of phosphoserine and phosphothreonine during acid hydrolysis. Anal Biochem. 73:1976;477-485.
12. Bordier C. Phase segregation of integral membrane proteins in Triton X-114 solution. J Biol Chem. 256:1981;1604-1607.
13. Casey P J. Protein lipidation in cell signaling. Science. 268:1995;221-225.
14. Schafer W R, Rine J. Protein prenylation. Annu Rev Genet. 30:1992;209-237.
15. Granger B L, Green S A, Gabel C A, Howe C L, Mellman I, Helenius A. Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells. J Biol Chem. 265:1990;12036-12043.
16. Bassett D E Jr, Boguski M S, Hieter P. Yeast genes and human diseases. Nature. 379:1996;589-590.