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PMID: 2454239 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Aspects of signal transduction in stimulus exocytosis-coupling in Paramecium.

Journal of cellular biochemistry ·Vol. 36 ·No. 4 ·1988-04-00 ·Pages 429-43

Satir BH, Busch G, Vuoso A, Murtaugh TJ

Abstract

This paper deals with the detailed mechanisms of signal transduction that lead to exocytosis during regulative secretion induced by specific secretagogues in a eukaryotic cell, Paramecium tetraurelia. There are at least three cellular compartments involved in the process: I) the plasma membrane, which contains secretagogue receptors and other transmembrane proteins, II) the cytoplasms, particularly in the region between the cell and secretory vesicle membranes, where molecules may influence interactions of the membranes, and III) the secretory vesicle itself. The ciliated protozoan Paramecium tetraurelia is very well suited for the study of signal transduction events associated with exocytosis because this eukaryotic cell contains thousands of docked secretory vesicles (trichocysts) below the cell membrane which can be induced to release synchronously when triggered with secretagogue. This ensures a high signal-to-noise ratio for events associated with this process. Upon release the trichocyst membrane fuses with the cell membrane and the trichocyst content undergoes a Ca2+-dependent irreversible expansion. Secretory mutants are available which are blocked at different points in the signal transduction pathway. Aspects of the three components mentioned above that will be discussed here include a) the properties of the vesicle content, its pH, and its membrane; b) the role of phosphorylation/dephosphorylation of a cytosolic 63-kilodalton (kDa)Mr protein in membrane fusion; and c) how influx of extracellular Ca2+ required for exocytosis may take place via exocytic Ca2+ channels which may be associated with specific membrane microdomains (fusion rosettes).

MeSH Terms
Animals Exocytosis Ion Channels/metabolism Membrane Fusion Microscopy, Electron Paramecium/physiology,ultrastructure Phosphoproteins/metabolism
Chemicals
Ion Channels Phosphoproteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Satir B H
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461.
Busch G
Vuoso A
Murtaugh T J
Article Info
Journal
Journal of cellular biochemistry
Abbr.
J Cell Biochem
ISSN
0730-2312
Published
1988-04-00
Pages
429-43
Language
English
Region
United States
NLM ID
8205768
Subset
IM
Grants
NCI NIH HHS · CA09475 · United States
NIGMS NIH HHS · GMO7128 · United States
NIGMS NIH HHS · GMS 32767 · United States
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