GTP-Binding proteins in brain and neutrophil are tethered to the plasma membrane via their amino termini

Brock Eide, Peter Gierschik, Graeme Milligan, Ian Mullaney, Cecilia Unson, Paul Goldsmith, Allen M. Spiegel

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a site near the amino-terminus, and quantitatively releases the large fragment (comprising all but an amino-terminal 2kDa piece) from the membrane. Our results indicate that alpha subunits are essentially cytoplasmic proteins tethered to the inner surface of the membrane via an amino terminal stalk.

Original languageEnglish (US)
Pages (from-to)1398-1405
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume148
Issue number3
DOIs
StatePublished - Nov 13 1987
Externally publishedYes

Fingerprint

Cell membranes
GTP-Binding Proteins
Brain
Neutrophils
Cell Membrane
GTP-Binding Protein alpha Subunits
Membranes
Guanosine Triphosphate
Trypsin
Immune Sera
Chemical activation
Peptides
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

GTP-Binding proteins in brain and neutrophil are tethered to the plasma membrane via their amino termini. / Eide, Brock; Gierschik, Peter; Milligan, Graeme; Mullaney, Ian; Unson, Cecilia; Goldsmith, Paul; Spiegel, Allen M.

In: Biochemical and Biophysical Research Communications, Vol. 148, No. 3, 13.11.1987, p. 1398-1405.

Research output: Contribution to journalArticle

Eide, Brock ; Gierschik, Peter ; Milligan, Graeme ; Mullaney, Ian ; Unson, Cecilia ; Goldsmith, Paul ; Spiegel, Allen M. / GTP-Binding proteins in brain and neutrophil are tethered to the plasma membrane via their amino termini. In: Biochemical and Biophysical Research Communications. 1987 ; Vol. 148, No. 3. pp. 1398-1405.
@article{40a63651cb9f46769a35f6b696854ee3,
title = "GTP-Binding proteins in brain and neutrophil are tethered to the plasma membrane via their amino termini",
abstract = "Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a site near the amino-terminus, and quantitatively releases the large fragment (comprising all but an amino-terminal 2kDa piece) from the membrane. Our results indicate that alpha subunits are essentially cytoplasmic proteins tethered to the inner surface of the membrane via an amino terminal stalk.",
author = "Brock Eide and Peter Gierschik and Graeme Milligan and Ian Mullaney and Cecilia Unson and Paul Goldsmith and Spiegel, {Allen M.}",
year = "1987",
month = "11",
day = "13",
doi = "10.1016/S0006-291X(87)80287-5",
language = "English (US)",
volume = "148",
pages = "1398--1405",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - GTP-Binding proteins in brain and neutrophil are tethered to the plasma membrane via their amino termini

AU - Eide, Brock

AU - Gierschik, Peter

AU - Milligan, Graeme

AU - Mullaney, Ian

AU - Unson, Cecilia

AU - Goldsmith, Paul

AU - Spiegel, Allen M.

PY - 1987/11/13

Y1 - 1987/11/13

N2 - Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a site near the amino-terminus, and quantitatively releases the large fragment (comprising all but an amino-terminal 2kDa piece) from the membrane. Our results indicate that alpha subunits are essentially cytoplasmic proteins tethered to the inner surface of the membrane via an amino terminal stalk.

AB - Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a site near the amino-terminus, and quantitatively releases the large fragment (comprising all but an amino-terminal 2kDa piece) from the membrane. Our results indicate that alpha subunits are essentially cytoplasmic proteins tethered to the inner surface of the membrane via an amino terminal stalk.

UR - http://www.scopus.com/inward/record.url?scp=0023652861&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023652861&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(87)80287-5

DO - 10.1016/S0006-291X(87)80287-5

M3 - Article

C2 - 2446610

AN - SCOPUS:0023652861

VL - 148

SP - 1398

EP - 1405

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -