Rab3D localizes to secretory granules in rat pancreatic acinar cells

European Journal of Cell Biology

Volumn 70, Issue 1, 1996, Pages 33-41

  Valentijn, Jack A ^a   Sengupta, Dola ^a   Gumkowski, Francine D ^a   Tang, Laura H ^a   Konieczko, Elisa M ^b   Jamieson, James D ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

Pancreatic acinar cells; Pancreatic islet cells; Rab3D; Regulated secretion; Secretory granules

Indexed keywords

ANTISERUM; GUANINE NUCLEOTIDE BINDING PROTEIN; OCTOXINOL; POLYCLONAL ANTIBODY; RAB PROTEIN; ZYMOGEN GRANULE;

ACINAR CELL; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; ELECTRON MICROSCOPY; IMMUNOBLOTTING; IMMUNOCYTOCHEMISTRY; IMMUNOGOLD STAINING; IMMUNOREACTIVITY; ISOELECTRIC FOCUSING; NONHUMAN; PANCREAS ISLET CELL; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; RAT; SECRETORY GRANULE; TWO DIMENSIONAL ELECTROPHORESIS;

EID: 0029892302     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (39)

1. Bailly, E., M. McCaffrey, N. Touchot, A. Zahraoui, B. Goud, M. Bornens: Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2. Nature 350, 715-718 (1991).
2. Baldini, G., T. Hohl, H. Y. Lin, H. F. Lodish: Cloning of a rab3 isotype predominantly expressed in adipocytes. Proc. Natl. Acad. Sci. USA 89, 5049-5052 (1992).
3. Baldini, G., P. E. Scherer, H. F. Lodish: Nonneuronal expression of Rab3A: Induction during adipogenesis and association with different intracellutar membranes than Rab3D. Proc. Natl. Acad. Sci. USA 92, 4284-4288 (1995).
4. Boguski, M.S., F. McCormick: Proteins regulating Ras and its relatives. Nature 366, 643-654 (1993).
5. Bordier, C.: Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256, 1604-1607 (1981).
6. Cameron, R. S., P. L. Cameron, J. D. Castle: A common spectrum of polypeptides occurs in secretion granule membranes of different exocrine glands J. Cell Biol. 103, 1299-1313 (1986).
7. Chavrier, P., R. G. Parton, H. P. Hauri, K. Simons, M. Zerial: Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62, 317-329 (1990)
8. De Camilli, P., S. M. Harris, W. B. Huttner, P. Greengard: Synapsin I (protein I), a nerve terminal specific phosphoprotein II. Its specific association with synaptic vesicles demonstrated by immunocytochemistry in agarose-embedded synaptosomes. J. Cell Biol. 96, 1355-1373 (1983).
9. Dirac-Svejstrup, A. B., T. Soldati, A. D. Shapiro, S. R. Pfeffer: Rab-GDI presents functional Rab9 to the intracellular transport machinery and contributes selectivity to Rab9 membrane recruitment. J. Biol. Chem. 269, 15427-15430 (1994).
10. Elferink, L. A., K. Anzai, R. H. Scheller: Rab15, a novel low molecular weight GTP-binding protein specifically expressed in rat brain. J. Biol. Chem. 267, 5768-5775 (1992).
11. Ferro-Novick, S., R. Jahn: Vesicle fusion from yeast to man Nature 370, 191-193 (1994).
12. Fischer von Mollard, G., G. A. Mignery, M. Baumert, M. S. Perin, T. J. Hanson, P. M. Burger, R. Jahn, T. C. Südhof: Rab3 is a small GTP-binding protein exclusively localized to synaptic vesicles. Proc. Natl. Acad. Sci. USA 87, 1988-1992 (1990).
13. Fischer von Mollard, G., B. Stahl, A. Khokhlatchev, T. C. Südhof, R. Jahn: Rab3C is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis. J. Biol. Chem. 269, 10971-10974 (1994).
14. Fischer von Mollard, G., B. Stahl, C. Walch-Solimena, K. Takei, L. Daniels, A. Khoklatchev, P. De Camilli, T. C. Südhof, R. Jahn: Localisation of Rab5 to synaptic vesicles identifies endosomal intermediate in synaptic vesicle recycling pathway. Eur. J. Cell Biol. 65, 319-326 (1994).
15. Fischer von Mollard, G., T. C. Südhof, R. Jahn: A small GTP-binding protein dissociates from synaptic vesicles during exocytosis. Nature 349, 79-81 (1991).
16. Gaisano, H. Y., L. Sheu, J. K. Foskett, W. S. Trimble: Tetanus toxin light chain cleaves a vesicle-associated membrane protein (VAMP) isoform 2 in rat pancreatic zymogen granules and inhibits enzyme secretion. J. Biol. Chem. 269, 17062-17066 (1994).
17. Glomset, J. A., C. C. Farnsworth: Role of protein modification reactions in programming interactions between Ras-related GTPase and cell membranes. Annu. Rev. Cell Biol. 10, 181-205 (1994).
18. Holz, R. W., W. H. Brondyk, R. A. Senter, L. Kuizon, I. G. Macara: Evidence for the involvement of Rab3A in Ca2+-dependent exocytosis from adrenal chromaffin cells. J. Biol. Chem. 269, 10229-10234 (1994)
19. Jena, B. P., F. D. Gumkowski, E. M. Konieczko, G. Fischer von Mollard, R. Jahn, J. D. Jamieson: Redistribution of a rab-3 like GTP binding protein from secretory granules to the Golgi complex in pancreatic acinar cells during regulated exocytosis. J. Cell Biol. 124, 43-53 (1994).
20. Karnieli, E., M. J. Zarnowski, P. J. Hissin, I. A. Simpson, L. B. Salans, S. W. Cushman: Insulin-stimulated translocation of glucose transport systems in the isolated rat adipose cell. J. Biol. Chem. 256, 4772-4777 (1981).
21. Karniguian, A., A. Zahraoui, A. Tavitian: Identification of small GTP-binding rab proteins in human platelets: Thrombin-induced phosphorylation of rab3B, rab6, and rab8 proteins. Proc. Natl. Acad. Sci. USA 90, 7647-7651 (1993).
22. Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1971).
23. Laurie, S. M., M. B. Mixon, J. D. Castle: GRAMP 100: A membrane protein concentrated on secretory membranes and the apical cell surface in exocrine acinar cells. J. Histochem. Cytochem. 40, 1827-1835 (1992).
24. Li, G., R. Regazzi, W. E. Balch, C. B. Wollheim: Stimulation of insulin release from permeabilized HIT-T15 cells by a synthetic peptide corresponding to the effector domain of the small GTP-binding protein rab3. FEBS Lett. 327, 145-149 (1993).
25. Lowry, O. H., N. J. Rosebrough, A. L. Farr, R. J. Randall: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275 (1951).
26. MacLean, C. M., G. J. Law, J. M. Edwardson: Stimulation of exocytotic membrane fusion by modified peptides of the rab3 effector domain: Re-evaluation of the role of rab3 in regulated exocytosis. Biochem J. 294, 325-328 (1993).
27. Martelli, A. M., R. Bareggi, G. Baldini, P. E. Scherer, H. F. Lodish: Diffuse vesicular distribution of Rab3D in the polarized neuroendocrine cell line AtT-20. FEBS Lett. 368, 271-275 (1995).
28. Matsui, Y., A. Kikuchi, S. Araki, Y. Hata, J. Kondo, Y. Teranishi, Y. Takai: Molecular cloning and characterization of a novel type of regulatory protein (GDI) for smg p25A, a ras p21-like GTP-binding protein. Mol. Cell. Biol. 10, 4116-4122 (1990).
29. Matteoli, M., K. Takei, R. Cameron, P. Hurlbut, P. A. Johnston, T. C. Sudhof, R. Jahn, P. De Camilli: Association of Rab3A with synaptic vesicles at late stages of the secretory pathway. J. Cell Biol. 115, 625-633 (1991).
30. O'Farrell, P. H.: High resolution two dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021 (1975).
31. Oberhauser, A. F., J. R. Monch, W. E. Balch, J. M. Fernandez: Exocytotic fusion is activated by Rab3a peptides. Nature 360, 270-273 (1992).
32. Padfield, P. J., W. E. Balch, J. D. Jamieson: A synthetic peptide of the rab3a effector domain stimulates amylase release from permeabilized pancreatic acini. Proc. Natl. Acad. Sci. USA 89, 1656-1660 (1992).
33. Schnefel, S., P. Zimmermann, A. Pröfrock, R. Jahn, K. Aktories, S. Zeuzem, W. Haase, I. Schulz: High- and small-molecular-weight GTP-binding proteins in zymogen granule membranes of rat pancreatic acinar cells. Cell Physiol. Biochem. 2, 77-89 (1992).
34. Senyshyn, J., W. E. Balch, R. W. Holz: Synthetic peptides of the effector-binding domain of rab enhance secretion from digitonin-permeabilized chromaffin cells. FEBS Lett. 309, 41-46 (1992).
35. Sogaard, M., K. Tani, R. R. Ye, S. Geromanos, P. Tempst, T. Kirchhausen, J. E. Rothman, T. Söllner: A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell 78, 937-948 (1994).
36. Su, Y.-C., L.-S. Kao, Y.-Y. Chu, Y. Liang, M.-H. Tsai, Y. Chern: Distribution and regulation of rab3C, a small molecular weight GTP-binding protein. Biochem. Biophys. Res. Commun. 200, 1257-1263 (1994).
37. Wagner, A. C. C., M. Z. Strowski, J. A. Williams: Identification of Rab 5 but not Rab 3A in rat pancreatic zymogen granule membranes. Biochem. Biophys. Res. Commun. 200, 542-548 (1994).
38. Weber, E., G. Berta, A. Tousson, P. St. John, M. W. Green, U. Gopalokrishnan, T. Jilling, E. J. Sorscher, T. S. Elton, D. R. Abrahamson, K. L. Kirk: Expression and polarized targeting of a Rab3 isoform in epithelial cells. J. Cell Biol. 125, 583-594 (1994).
39. Zeuzem, S., D. Stryjek-Kaminska, W. F. Caspary, J. Stein, A. Piiper: Effect of a Rab3A effector domain-related peptide, CCK, and EGF in permeabilized pancreatic acini. Am. J. Physiol. Gastrointest. Liver Physiol. 267, G350-G356 (1994).