Literature DB >> 2454239

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

B H Satir1, G Busch, A Vuoso, T J Murtaugh.   

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).

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Year:  1988        PMID: 2454239     DOI: 10.1002/jcb.240360411

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  8 in total

Review 1.  The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release.

Authors:  P J Robinson
Journal:  Mol Neurobiol       Date:  1991       Impact factor: 5.590

2.  Species distribution of a phosphoprotein (parafusin) involved in exocytosis.

Authors:  B H Satir; T Hamasaki; M Reichman; T J Murtaugh
Journal:  Proc Natl Acad Sci U S A       Date:  1989-02       Impact factor: 11.205

3.  Carbohydrate cycling in signal transduction: parafusin, a phosphoglycoprotein and possible Ca(2+)-dependent transducer molecule in exocytosis in Paramecium.

Authors:  S V Subramanian; B H Satir
Journal:  Proc Natl Acad Sci U S A       Date:  1992-12-01       Impact factor: 11.205

4.  Cloning and sequencing of parafusin, a calcium-dependent exocytosis-related phosphoglycoprotein.

Authors:  S V Subramanian; E Wyroba; A P Andersen; B H Satir
Journal:  Proc Natl Acad Sci U S A       Date:  1994-10-11       Impact factor: 11.205

5.  Lysozyme acts as a chemorepellent and secretagogue in Paramecium by activating a novel receptor-operated Ca++ conductance.

Authors:  T M Hennessey; M Y Kim; B H Satir
Journal:  J Membr Biol       Date:  1995-11       Impact factor: 1.843

6.  Quenched flow analysis of exocytosis in Paramecium cells: time course, changes in membrane structure, and calcium requirements revealed after rapid mixing and rapid freezing of intact cells.

Authors:  G Knoll; C Braun; H Plattner
Journal:  J Cell Biol       Date:  1991-06       Impact factor: 10.539

7.  A Ca2+ influx associated with exocytosis is specifically abolished in a Paramecium exocytotic mutant.

Authors:  D Kerboeuf; J Cohen
Journal:  J Cell Biol       Date:  1990-12       Impact factor: 10.539

8.  Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver.

Authors:  B H Satir; C Srisomsap; M Reichman; R B Marchase
Journal:  J Cell Biol       Date:  1990-09       Impact factor: 10.539

  8 in total

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