J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/06/1161/09 $2.00
Volume 137, Number 5, June 2, 1997 1161-1169

Different Steady State Subcellular Distributions of the Three Splice Variants of Lysosome-associated Membrane Protein LAMP-2 Are Determined Largely by the COOH-terminal Amino Acid Residue

Nancy R. Gough, and Douglas M. Fambrough

Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218

The extensively glycosylated lysosome-associated membrane proteins (LAMP)-2a, b, and c are derived from a single gene by alternative splicing that produces proteins with differences in the transmembrane and cytosolic domains. The lysosomal targeting signals reside in the cytosolic domain of these proteins. LAMPs are not restricted to lysosomes but can also be found in endosomes and at the cell surface. We investigated the subcellular distribution of chimeras comprised of the lumenal domain of avian LAMP-1 and the alternatively spliced domains of avian LAMP-2. Chimeras with the LAMP-2c cytosolic domain showed predominantly lysosomal distribution, while higher levels of chimeras with the LAMP-2a or b cytosolic domain were present at the cell surface. The increase in cell surface expression was due to differences in the recognition of the targeting signals and not saturation of intracellular trafficking machinery. Site-directed mutagenesis defined the COOH-terminal residue of the cytosolic tail as critical in governing the distributions of LAMP-2a, b, and c between intracellular compartments and the cell surface.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R., Cuervo, A. M. (2006). Consequences of the selective blockage of chaperone-mediated autophagy. Proc. Natl. Acad. Sci. USA 103: 5805-5810 [Abstract] [Full Text]  
• Rous, B. A., Reaves, B. J., Ihrke, G., Briggs, J. A.G., Gray, S. R., Stephens, D. J., Banting, G., Luzio, J. P. (2002). Role of Adaptor Complex AP-3 in Targeting Wild-Type and Mutated CD63 to Lysosomes. Mol. Biol. Cell 13: 1071-1082 [Abstract] [Full Text]  
• Kuronita, T., Eskelinen, E.-L., Fujita, H., Saftig, P., Himeno, M., Tanaka, Y. (2002). A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology. J. Cell Sci. 115: 4117-4131 [Abstract] [Full Text]  
• Obermuller, S., Kiecke, C., von Figura, K., Honing, S. (2002). The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targetting to lysosomes. J. Cell Sci. 115: 185-194 [Abstract] [Full Text]  
• Husain, M., Moss, B. (2001). Vaccinia Virus F13L Protein with a Conserved Phospholipase Catalytic Motif Induces Colocalization of the B5R Envelope Glycoprotein in Post-Golgi Vesicles. J. Virol. 75: 7528-7542 [Abstract] [Full Text]  
• Fratti, R. A., Backer, J. M., Gruenberg, J., Corvera, S., Deretic, V. (2001). Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest. J. Cell Biol. 154: 631-644 [Abstract] [Full Text]  
• Di Cristina, M., Spaccapelo, R., Soldati, D., Bistoni, F., Crisanti, A. (2000). Two Conserved Amino Acid Motifs Mediate Protein Targeting to the Micronemes of the Apicomplexan Parasite Toxoplasma gondii. Mol. Cell. Biol. 20: 7332-7341 [Abstract] [Full Text]  
• Cuervo, A., Dice, J. (2000). Unique properties of lamp2a compared to other lamp2 isoforms. J. Cell Sci. 113: 4441-4450 [Abstract]  
• Harb, O. S., Abu Kwaik, Y. (2000). Characterization of a Macrophage-Specific Infectivity Locus (milA) of Legionella pneumophila. Infect. Immun. 68: 368-376 [Abstract] [Full Text]  
• Brown, D, Breton, S (2000). H(+)V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: vesicle recycling and transcytotic pathways. J. Exp. Biol. 203: 137-145 [Abstract]  
• Gough, N., Zweifel, M., Martinez-Augustin, O, Aguilar, R., Bonifacino, J., Fambrough, D. (1999). Utilization of the indirect lysosome targeting pathway by lysosome-associated membrane proteins (LAMPs) is influenced largely by the C-terminal residue of their GYXXphi targeting signals. J. Cell Sci. 112: 4257-4269 [Abstract]  
• Ohno, H., Aguilar, R. C., Yeh, D., Taura, D., Saito, T., Bonifacino, J. S. (1998). The Medium Subunits of Adaptor Complexes Recognize Distinct but Overlapping Sets of Tyrosine-based Sorting Signals. J. Biol. Chem. 273: 25915-25921 [Abstract] [Full Text]  
• Beers, M. F., Lomax, C. A., Russo, S. J. (1998). Synthetic Processing of Surfactant Protein C by Alevolar Epithelial Cells. THE COOH TERMINUS OF proSP-C IS REQUIRED FOR POST-TRANSLATIONAL TARGETING AND PROTEOLYSIS. J. Biol. Chem. 273: 15287-15293 [Abstract] [Full Text]  
• Reaves, B. J., Banting, G., Luzio, J. P. (1998). Lumenal and Transmembrane Domains Play a Role in Sorting Type I Membrane Proteins on Endocytic Pathways. Mol. Biol. Cell 9: 1107-1122 [Abstract] [Full Text]  
• Kain, R., Angata, K., Kerjaschki, D., Fukuda, M. (1998). Molecular Cloning and Expression of a Novel Human trans-Golgi Network Glycoprotein, TGN51, That Contains Multiple Tyrosine-containing Motifs. J. Biol. Chem. 273: 981-988 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents