Abstract
LOW-MOLECULAR-WEIGHT GTP-binding proteins (small G proteins) of the Rab family have been proposed to act as central regulators of vesicular traffic1,2, and proteins of the Rab3 subfamily (Rab3A, B, C and D)3–6 are thought to be associated with membrane vesicles or granules undergoing exocytotic fusion with the plasma membrane7–10. Rab3A is highly expressed in brain11, whereas Rab3B is the major form found in rat anterior pituitary gland. We report here that antisense oligonucleotides against Rab3B, introduced into pituitary cells using the whole-cell patch clamp technique, specifically and reversibly block expression of Rab3B. We find that calcium-dependent exocytosis is inhibited without affecting endocytosis. Antisense oligonucleotides directed against Rab3A have no effect. Our results indicate that Rab3B is likely to be a key intracellular signalling molecule which can control exocytosis downstream of other calcium-dependent processes in anterior pituitary cells.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Goud, B., Salminen, A., Walworth, A. & Novick, P. J. Cell 53, 753–768 (1988).
Bourne, H. R. Cell 53, 669–670 (1988).
Touchot, N., Chardin, P. & Tavitian, A. Proc. natn. Acad. Sci. U.S.A. 84, 8210–8214 (1987).
Matsui, Y. et al. J. biol. Chem. 263, 11071–11074 (1988).
Zahraoui, A., Touchot, N., Chardin, P. & Tavitian A. Nucleic Acids Res. 16, 1204 (1988).
Baldini, G., Hohl, T., Lin, H. Y. & Lodish, H. F. Proc. natn. Acad. Sci. U.S.A. 89, 5049–5052 (1992).
Fischer von Mollard, G. et al. Proc. natn. Acad. Sci. U.S.A. 87, 1988–1992 (1990).
Darchen, F. et al. Proc. natn. Acad. Sci. U.S.A. 87, 5692–5696 (1990).
Mizoguchi, A. et al. J. biol. Chem. 265, 11872–11879 (1990).
Oberhauser, A. F., Monck, J. R., Balch, W. E. & Fernandez, J. M. Nature 360, 270–273 (1992).
Ayala, J., Olofsson, B., Tavitian, A. & Prochiantz, A. J. Neurosci. Res. 22, 241–246 (1989).
Taraskevich, P. S. & Douglas, W. W. Fed. Proc. 43, 2373–2378 (1984).
Valencia, A., Chardin, P., Wittinghofer, A. & Sander, C. Biochemistry 30, 4637–4648 (1991).
Pfeffer, S. R. Trends Cell Biol. 2, 41–46 (1992).
Baertschi, A. J., Audigier, Y., Lledo, P. M., Israel, J.-M. & Vincent, J.-D. Molec. Endocrin. 6, 2257–2265 (1992).
Sikdar, S. K., Zorec, R., Brown, D. & Mason, W. T. FEBS Lett. 253, 88–92 (1989).
Thomas, P., Surprenant, A. & Aimers, W. Neuron 5, 723–733 (1990).
Zorec, R., Sikdar, S. K. & Mason, W. T. J. gen. Physiol. 97, 473–497 (1991).
Von Grafenstein, H., Roberts, C. S. & Baker, P. F. J. Cell. Biol. 103, 2343–2352 (1986).
Rupnik, R. & Zorec, R. FEBS Lett. 303, 221–223 (1992).
Plutner, H., Schwaninger, R., Pind, S. & Balch, W. E. EMBO J. 9, 2375–2383 (1990).
Van der Sluijs, P. et al. Cell 70, 729–740 (1992).
Gorvel, J. P., Chavrier, P., Zerial, M. & Gruenberg, J. Cell 64, 915–925 (1991).
Bucci, C. et al. Cell 70, 715–728 (1992).
Regazzi, R., Kikuchi, A., Takai, Y. & Wollheim, C. B. J. biol. Chem. 267, 17512–17519 (1992).
Bourne, H. R., Sanders, D. A. & McCormick, F. Nature 348, 125–132 (1990).
Takai, Y., Kaibuchi, K., Kikuchi, A. & Kawata, M. Int. Rev. Cytol. 133, 187–230 (1992).
Senyshyn, J., Balch, W. E. & Holz, R. W. FEBS Lett. 309, 41–46 (1992).
Padfield, P. J., Balch, W. E. & Jamieson, J. D. Proc. natn. Acad. Sci. U.S.A. 89, 1656–1660 (1992).
Mason, W. T. & Ingram, C. D. Meth. Enzym. 124, 207–242 (1986).
Neher, E. & Marty, A. Proc. natn. Acad. Sci. U.S.A. 79, 6712–6716 (1982).
Marty, A. & Neher, E. Single-channel Recording (eds Sakmann, B. & Neher, E.) 107–121 (Plenum, New York, 1983).
Push, M. & Neher, E. Pflügers Archs 411, 204–211 (1988).
Zorec, R., Henigman, F., Mason, W. T. & Kordaš, M. Meth. Neurosci. 4, 194–210 (1991).
Lindau, M. & Neher, E. Pflügers Archs 411, 137–146 (1988).
Grynkiewicz, G., Poenie, M. & Tsien, R. Y. J. biol. Chem. 260, 3440–3450 (1985).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Lledo, PM., Verniert, P., Vincent, JD. et al. Inhibition of RabSB expression attenuates Ca2+-dependent exocytosis in rat anterior pituitary cells. Nature 364, 540–544 (1993). https://doi.org/10.1038/364540a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/364540a0
This article is cited by
-
Elevated expression of RAB3B plays important roles in chemoresistance and metastatic potential of hepatoma cells
BMC Cancer (2022)
-
Identification of transcriptome alterations in the prefrontal cortex, hippocampus, amygdala and hippocampus of suicide victims
Scientific Reports (2021)
-
Secretory RAB GTPase 3C modulates IL6-STAT3 pathway to promote colon cancer metastasis and is associated with poor prognosis
Molecular Cancer (2017)
-
High-resolution membrane capacitance measurements for the study of exocytosis and endocytosis
Nature Protocols (2013)
-
Functional molecular morphology of anterior pituitary cells, from hormone production to intracellular transport and secretion
Medical Molecular Morphology (2011)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.