TGN38 cycles via the basolateral membrane of polarized Caco-2 cells

References

• Brewer C. B., Roth M. A single amino-acid change in the cytoplasmic domain alters the polarized delivery of influenza-virus hemagglutinin. Journal of Cell Biology 1991; 114: 413–421
   PubMed Web of Science ®Google Scholar
• LeBivic A., Sambury Y., Patzak A., Patil N., Chao M., Rodriguez-Boulan E. An internal deletion in the cytoplasmic tail reverses the apical localization of human NGF receptor in transfected MDCK cells. Journal of Cell Biology 1991; 115: 607–618
   PubMed Web of Science ®Google Scholar
• Matter K., Yamamoto E. M., Mellman I. Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL-receptors and Fc-receptors in MDCK cells. Journal of Cell Biology 1994; 126: 991–1004
   PubMed Web of Science ®Google Scholar
• Prill V., Lehmann L., von Figura K., Peters C. The cytoplasmic tail of lysosomal acid-phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells. The EMBO Journal 1993; 12: 2181–2193
   PubMed Web of Science ®Google Scholar
• Aroeti B., Kosen P. A., Kuntz I. D., Cohen F. E., Mostov K. E. Mutational and secondary structural-analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor. Journal of Cell Biology 1993; 123: 1149–1160
   PubMed Web of Science ®Google Scholar
• Matter K., Whitney J. A., Yamamoto E. M., Mellman I. Common signals control low-density-lipoprotein receptor sorting in endosomes and the Golgi-complex of MDCK cells. Cell 1993; 74: 1053–1064
   PubMed Web of Science ®Google Scholar
• Lin S., Nairn H. Y., Roth M. Tyrosine-dependent basolateral sorting signals are distinct from tyrosine dependent internalization signals. Journal of Biological Chemistry 1997; 272(26)300–26; 305
   Google Scholar
• Scheiffele P., Peranen J., Simons K. N-glycans as apical sorting signals in epithelial-cells. Nature 1995; 378: 96–98
   PubMed Web of Science ®Google Scholar
• Gut A., Kappeler F., Hyka N., Balda M. S., Hauri H.-P, Matter K. Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins. The EMBO Journal 1998; 17: 1919–1929
   PubMed Web of Science ®Google Scholar
• Casanova J. E., Breitfeld P. P., Ross S. A., Mostov K. E. Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis. Science 1990; 248: 742–745
   PubMed Web of Science ®Google Scholar
• Banting G., Ponnambalam S. TGN38 and its orthologues: roles in post-TGN vesicle formation and maintenance of TGN morphology. Biochemica et Biophysics Acta Molecular Cell Research 1997; 1355: 209–217
   PubMed Web of Science ®Google Scholar
• Luzio J. P., Brake B., Banting G., Howell K. E., Bragnetta P., Stanley K. K. Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN 38). Biochemical Journal 1990; 270: 97–102
   PubMed Web of Science ®Google Scholar
• Ponnambalam S., Girotti M., Yaspo M. L, Owen C. W., Perry A. C. F., Suganuma T., Nilsson T., Fried M., Banting G., Warren G. Primate homologues of rat TGN38: primary structure, expression and functional implications. Journal of Cell Science 1996; 109: 675–685
   PubMed Web of Science ®Google Scholar
• Girotti M., Banting G. TGN38-Green Fluorescent Protein hybrid proteins expressed in stably transfected eukaryotic cells provide a tool for the real-time, in vivo study of membrane traffic pathways and suggest a possible role for rat TGN38. Journal of Cell Science 1996; 109: 2915–2926
   PubMed Web of Science ®Google Scholar
• Jones S. M., Crosby J. R., Salamero J., Howell K. E. A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. Journal of Cell Biology 1993; 122: 775–788
   PubMed Web of Science ®Google Scholar
• Kasai K., Takahashi S., Murakami K., Nakayama K. Strain-specific presence of 2 TGN38 isoforms and absence of TGN41 in mouse. Journal of Biological Chemistry 1995; 270(14)471–14; 476
   Google Scholar
• Kain R., Angata K., Kerjaschki D., Fukuda M. Molecular cloning and expression of a novel human trans-Golgi network glycoprotein, TGN51, that contains multiple tyrosine-containing motifs. Journal of Biological Chemistry 1998; 273: 981–988
   PubMed Web of Science ®Google Scholar
• Ponnambalam S., Rabouille C., Luzio J. P., Nilsson T., Warren G. The TGN38 glycoprotein contains 2 non-overlapping signals that mediate localization to the trans-Golgi network. Journal of Cell Biology 1994; 125: 253–268
   PubMed Web of Science ®Google Scholar
• Rajasekaran A. K., Humphrey J. S., Wagner M., Miesenbock G., Lebivic A., Bonifacino J. S., Rodriguez-Boulan E. TGN38 recycles basolaterally in polarized Madin-Darby Canine Kidney cells. Molecular Biology of the Cell 1994; 5: 1093–1103
   PubMed Web of Science ®Google Scholar
• Fogh J., Wright W. C., Loveless J. D. Absence of Hela cell contamination in 169 cell lines derived from human tumors. Journal of the National Cancer Institute 1977; 58: 209–214
   PubMed Web of Science ®Google Scholar
• Le Bivic A., Quaroni A., Nichols B., Rodriguez-Boulan E. Biogenetic pathways of plasma-membrane proteins in Caco-2, a human intestinal epithelial-cell line. Journal of Cell Biology 1990; 111: 1351–1361
   PubMed Web of Science ®Google Scholar
• Matter K., Brauchbar M., Bucher K., Hauri H.-P. Sorting of endogenous plasma-membrane proteins occurs from 2 sites in cultured human intestinal epithelial-cells (Caco-2). Cell 1990; 60: 429–437
   PubMed Web of Science ®Google Scholar
• Horn M., Banting G. Okadaic acid treatment leads to a fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell-surface. Biochemical Journal 1994; 301: 69–73
   PubMed Web of Science ®Google Scholar
• Reaves B., Banting G. Perturbation of the morphology of the trans-Golgi network following brefeldin-A treatment-redistribution of aTGN-specific integral membrane-protein, TGN38. Journal of Cell Biology 1992; 116: 85–94
   PubMed Web of Science ®Google Scholar
• Bacallao R., Antony C., Dotti C., Karsenti E., Stelzer E. H. K., Simons K. The subcellular organization of Madin-Darby Canine Kidney cells during the formation of a polarized epithelium. Journal of Cell Biology 1989; 109: 2817–2832
   PubMed Web of Science ®Google Scholar
• Reaves B., Horn M., Banting G. TGN38/41 recycles between the cell-surface and the TGN—Brefeldin-A affects its rate of return to the TGN. Molecular Biology of the Ceil 1993; 4: 93–105
   PubMed Web of Science ®Google Scholar
• Ladinsky M. S., Howell K. E. An electron-microscopic study of TGN38/41 dynamics. Journal of Cell Science 1993; 41–47
   PubMed Web of Science ®Google Scholar
• Ellis J. A., Luzio J. P. Identification and characterization of a novel protein (p137) which transcytoses bidirectionally in Caco-2 cells. Journal of Biological Chemistry 1995; 270: 21717–21723
   Web of Science ®Google Scholar
• Reaves B., Banting G. Overexpression of TGN38/41 leads to mislocalization of gamma-adaptin. FEBS Letters 1994; 351: 448–456
   PubMed Web of Science ®Google Scholar