Home LiteratureArticle Details
PMID: 2915987 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

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

Satir BH, Hamasaki T, Reichman M, Murtaugh TJ

Abstract

A cytosolic phosphoprotein that appears to function in membrane fusion during exocytosis of secretory products has previously been isolated from Paramecium tetraurelia. This phosphoprotein, parafusin, with Mr 63,000, is rapidly dephosphorylated via a Ca2+-dependent process when secretagogues induce exocytosis in competent cells. Dephosphorylation does not occur in exocytosis-incompetent cells. Polyclonal antibodies against purified parafusin have now been used to show that this protein is present in unicellular organisms and cells of metazoan groups of wide evolutionary divergence, such as yeast, insects, and mammals, including humans. These results suggest that parafusin was present early in the history of eukaryotes and that it is of functional importance in the general mechanism of exocytosis and membrane fusion.

MeSH Terms
Animals Cross Reactions Exocytosis Humans Immunoblotting Molecular Weight Paramecium/physiology Phosphoproteins/isolation & purification,physiology Species Specificity
Chemicals
Phosphoproteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Satir B H
Department of Anatomy & Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461.
Hamasaki T
Reichman M
Murtaugh T J
References (8)
8 references, click to expand
  1. Mutations affecting the trichocysts in Paramecium aurelia. I. Morphology and description of the mutants.
    J Protozool. 1974 May;21(2):352-62 PMID: 4599165
  2. Genetic analysis of membrane differentiation in Paramecium. Freeze-fracture study of the trichocyst cycle in wild-type and mutant strains.
    J Cell Biol. 1976 Apr;69(1):126-43 PMID: 1254639
  3. Protein phosphorylation/dephosphorylation and stimulus-secretion coupling in wild type and mutant Paramecium.
    J Biol Chem. 1982 Dec 10;257(23):13903-6 PMID: 7142183
  4. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  5. Purification of and production of an antibody against a 63,000 Mr stimulus-sensitive phosphoprotein in Paramecium.
    J Biol Chem. 1987 Nov 15;262(32):15734-9 PMID: 3680223
  6. Aspects of signal transduction in stimulus exocytosis-coupling in Paramecium.
    J Cell Biochem. 1988 Apr;36(4):429-43 PMID: 2454239
  7. Localization of the glucose phosphotransferase to a cytoplasmically accessible site on intracellular membranes.
    J Biol Chem. 1988 Nov 25;263(33):17792-7 PMID: 2846578
  8. Synchronous exocytosis in Paramecium cells involves very rapid (less than or equal to 1 s), reversible dephosphorylation of a 65-kD phosphoprotein in exocytosis-competent strains.
    J Cell Biol. 1985 Dec;101(6):2028-35 PMID: 4066748
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1989-02-00
Pages
930-2
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC286592
Subset
IM
Grants
NIGMS NIH HHS · GM32762 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com