Species distribution of a phosphoprotein (parafusin) involved in exocytosis

Birgit H. Satir, T. Hamasaki, M. Reichman, T. J. Murtaugh

Research output: Contribution to journalArticle

22 Citations (Scopus)

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 M(r) 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.

Original languageEnglish (US)
Pages (from-to)930-932
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number3
StatePublished - 1989

Fingerprint

Phosphoproteins
Exocytosis
Membrane Fusion
Paramecium tetraurelia
Eukaryota
Insects
Mammals
Yeasts
History
Antibodies
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Species distribution of a phosphoprotein (parafusin) involved in exocytosis. / Satir, Birgit H.; Hamasaki, T.; Reichman, M.; Murtaugh, T. J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 86, No. 3, 1989, p. 930-932.

Research output: Contribution to journalArticle

Satir, Birgit H. ; Hamasaki, T. ; Reichman, M. ; Murtaugh, T. J. / Species distribution of a phosphoprotein (parafusin) involved in exocytosis. In: Proceedings of the National Academy of Sciences of the United States of America. 1989 ; Vol. 86, No. 3. pp. 930-932.
@article{fb0d2dfcd4b14b8abdc5aef09726b8ff,
title = "Species distribution of a phosphoprotein (parafusin) involved in exocytosis",
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 M(r) 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.",
author = "Satir, {Birgit H.} and T. Hamasaki and M. Reichman and Murtaugh, {T. J.}",
year = "1989",
language = "English (US)",
volume = "86",
pages = "930--932",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "3",

}

TY - JOUR

T1 - Species distribution of a phosphoprotein (parafusin) involved in exocytosis

AU - Satir, Birgit H.

AU - Hamasaki, T.

AU - Reichman, M.

AU - Murtaugh, T. J.

PY - 1989

Y1 - 1989

N2 - 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 M(r) 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.

AB - 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 M(r) 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.

UR - http://www.scopus.com/inward/record.url?scp=0024581733&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024581733&partnerID=8YFLogxK

M3 - Article

C2 - 2915987

AN - SCOPUS:0024581733

VL - 86

SP - 930

EP - 932

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 3

ER -