Golgi protein

Deficient animals are also more susceptible to infection than are adequately nourished control animals, with impaired antibody responses. This seems to be due to a defect in the transport of proteins destined for export from the cell as a result of the impairment of acylation of Golgi proteins. 

Cole NB, Smith CL, Sciaky N, Terasaki M, Edidin M, Lippincott-Schwartz J. Diffusional mobility of Golgi proteins in membranes of living cells. Science 1996 273 797—801. 

Lippincott-Schwartz J, Yuan LC, Bonitacino JS, et ol. (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A Evidence for membrane cycling from the Golgi to the ER. In Cell 56 801 -813. 

Duden, R., Hosobuchi, M., Hamamoto, S., Winey, M., Byers, B., andSchekman, R. (1994). Yeast beta- and beta -coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic./. Biol. Chem. 269, 24486-24495. 

Santos, B., and Snyder, M. (2000). Sbe2p and sbe22p, two homologous Golgi proteins involved in yeast cell wall formation. Mol. Biol. Cell 11, 435-452. 

R.W. Dorns, G. Russ, J.W. Yewdell, Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum, /. Cell Biol. 1989, 109, 61-72. 

VPS33 Post-Golgi protein sorting Deficient post-Golgi sorting/apoFet3p... 

Martinez, O., Antony, C., Pehau-Arnaudet, G., Berger, E. G., Salamero, J., and Goud, B (1997). GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 94,1828-1833. 

Yang, W., and Storrie, B. (1998). Scattered Golgi elements during microtubule disruption are initially emiched in trans-Golgi proteins. Mol Biol. Cell 9,191-207. 

Marra, P., Maffucci, T., Daniele, T., TuUio, G. D., Ikehara, Y., Chan, E. K., Luini, A., Beznoussenko, G., Mironov, A., and De Matteis, M. A. (2001). The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment. Nat. Cell Biol 3,1101-1113. 

Lesa, G. M., Seemann, J., Shorter, J., Vandekerckhove, J., and Warren, G. (2000). The amino-terminal domain of the golgi protein giantin interacts directly with the vesicle-tethering protein pll5. J. Biol. Chem. 275, 2831-2836. 

This approach can also be used to identify novel or unexpected proteins that contribute to cytoskeletal function on membranes. We have successfully isolated and identified individual protein bands from the SDS-PAGE gels and identified them using mass spectrometry (Chen et al., 2004). This has been particularly feasible with the vesicle fractions and liposome binding assays where the background from resident Golgi proteins is greatly reduced or absent (Fig. 3). 

Much progress has been made in identifying Man-T genes and defining the roles of their products various biosynthetic pathways. Man-T will be discussed in the context of the secretory pathway of eukaryotic cells and the biosynthetic pathways that are localized in the ER and Golgi. Proteins related by amino acid sequence... 

S. Munro, An investigation of the role of transmembrane domains in Golgi protein retention, EMBO J, 1995, 14, 4695-4704. 

---