Short transmembrane domains with high-volume exoplasmic halves determine retention of type II membrane proteins in the golgi complex

Journal of Cell Science

Volumn 126, Issue 23, 2013, Pages 5344-5349

  Quiroga, Rodrigo ^a   Trenchi, Alejandra ^a   Montoro, Ayelén González ^a   Taubas, Javier Valdez ^a   Maccioni, Hugo J F ^a  

^a UNIVERSIDAD NACIONAL DE CÓRDOBA   (Argentina)

Author keywords

Golgi; SNAREs; Traffic; Transmembrane domain; Yeast

Indexed keywords

CELL MEMBRANE PROTEIN; SNARE PROTEIN;

AMINO ACID COMPOSITION; ARTICLE; CELL MEMBRANE; CELLULAR DISTRIBUTION; CHIMERA; CYTOPLASM; GOLGI COMPLEX; HYDROPHOBICITY; MAMMAL CELL; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; SACCHAROMYCES CEREVISIAE; TRANS GOLGI NETWORK; TRANSMEMBRANE DOMAIN; YEAST;

GOLGI; SNARES; TRAFFIC; TRANSMEMBRANE DOMAIN; YEAST;

AMINO ACID SEQUENCE; ANIMALS; CELL MEMBRANE; CHO CELLS; CRICETULUS; GENE EXPRESSION REGULATION, FUNGAL; GOLGI APPARATUS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; QA-SNARE PROTEINS; QC-SNARE PROTEINS; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84890218898     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.130658     Document Type: Article

References (24)

1. Aalto, M. K., Ronne, H. and Keränen, S. (1993). Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. EMBO J. 12, 4095-4104.
2. Aoki, D., Lee, N., Yamaguchi, N., Dubois, C. and Fukuda, M. N. (1992). Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain. Proc. Natl. Acad. Sci. USA 89, 4319-4323.
3. Banfield, D. K., Lewis, M. J. and Pelham, H. R. (1995). A SNARE-like protein required for traffic through the Golgi complex. Nature 375, 806-809.
4. Bretscher, M. S. and Munro, S. (1993). Cholesterol and the Golgi apparatus. Science 261, 1280-1281.
5. Duran, J. M., Campelo, F., van Galen, J., Sachsenheimer, T., Sot, J., Egorov, M. V., Rentero, C., Enrich, C., Polishchuk, R. S., Goñi, F. M. et al. (2012). Sphingomyelin organization is required for vesicle biogenesis at the Golgi complex. EMBO J. 31, 4535-4546.
6. Engelman, D. M., Steitz, T. A. and Goldman, A. (1986). Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15, 321-353.
7. Giraudo, C. G., Daniotti, J. L. and Maccioni, H. J. F. (2001). Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus. Proc. Natl. Acad. Sci. USA 98, 1625-1630.
8. Gomez, G. A. and Daniotti, J. L. (2005). H-Ras dynamically interacts with recycling endosomes in CHO-K1 cells: involvement of Rab5 and Rab11 in the trafficking of HRas to this pericentriolar endocytic compartment. J. Biol. Chem. 280, 34997-35010.
9. Herzig, Y., Sharpe, H. J., Elbaz, Y., Munro, S. and Schuldiner, M. (2012). A systematic approach to pair secretory cargo receptors with their cargo suggests a mechanism for cargo selection by Erv14. PLoS Biol. 10, e1001329.
10. Klemm, R. W., Ejsing, C. S., Surma, M. A., Kaiser, H.-J., Gerl, M. J., Sampaio, J. L., de Robillard, Q., Ferguson, C., Proszynski, T. J., Shevchenko, A. et al. (2009). Segregation of sphingolipids and sterols during formation of secretory vesicles at the trans-Golgi network. J. Cell Biol. 185, 601-612.
11. Maccioni, H. J. F., Quiroga, R. and Spessott, W. (2011). Organization of the synthesis of glycolipid oligosaccharides in the Golgi complex. FEBS Lett. 585, 1691-1698.
12. Munro, S. (1995). An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J. 14, 4695-4704.
13. Nikolovski, N., Rubtsov, D., Segura, M. P., Miles, G. P., Stevens, T. J., Dunkley, T. P. J., Munro, S., Lilley, K. S. and Dupree, P. (2012). Putative glycosyltransferases and other plant Golgi apparatus proteins are revealed by LOPIT proteomics. Plant Physiol. 160, 1037-1051.
14. Opat, A. S., van Vliet, C. and Gleeson, P. A. (2001). Trafficking and localisation of resident Golgi glycosylation enzymes. Biochimie 83, 763-773.
15. Polishchuk, E. V., Di Pentima, A., Luini, A. and Polishchuk, R. S. (2003). Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains. Mol. Biol. Cell 14, 4470- 4485.
16. Rayner, J. C. and Pelham, H. R. (1997). Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16, 1832-1841.
17. Ronchi, P., Colombo, S., Francolini, M. and Borgese, N. (2008). Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum. J. Cell Biol. 181, 105-118.
18. Sharpe, H. J., Stevens, T. J. and Munro, S. (2010). A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 142, 158-169.
19. Sousa, V. L., Brito, C., Costa, T., Lanoix, J., Nilsson, T. and Costa, J. (2003). Importance of Cys, Gln, and Tyr from the transmembrane domain of human alpha 3/4 fucosyltransferase III for its localization and sorting in the Golgi of baby hamster kidney cells. J. Biol. Chem. 278, 7624-7629.
20. Tang, B. L., Wong, S. H., Low, S. H. and Hong, W. (1992). The transmembrane domain of N-glucosaminyltransferase I contains a Golgi retention signal. J. Biol. Chem. 267, 10122-10126.
21. Teasdale, R. D., D'Agostaro, G. and Gleeson, P. A. (1992). The signal for Golgi retention of bovine beta 1,4-galactosyltransferase is in the transmembrane domain. J. Biol. Chem. 267, 13113.
22. Tsai, J., Taylor, R., Chothia, C. and Gerstein, M. (1999). The packing density in proteins: standard radii and volumes. J. Mol. Biol. 290, 253-266.
23. Tu, L., Tai, W. C. S., Chen, L. and Banfield, D. K. (2008). Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science 321, 404-407.
24. Valdez-Taubas, J. and Pelham, H. R. (2003). Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling. Curr. Biol. 13, 1636-1640.