Cytoskeletal association of the cholera toxin receptor in rat erythrocytes

Naji Sahyoun; Talal Shatila; Harry Levine; Pedro Cuatrecasas

doi:10.1016/S0006-291X(81)80141-6

Cytoskeletal association of the cholera toxin receptor in rat erythrocytes

Naji Sahyoun
, Talal Shatila
, Harry Levine
, Pedro Cuatrecasas

Molecular and Cellular Biochemistry

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Cholera toxin receptors are associated with the cytoskeletal residue of Triton X-100 extracts of rat erythrocytes. The solubilized cytoskeletal toxin-receptor complex appears to be a large macromolecular entity whose formation is facilitated by increased receptor occupancy. These findings suggest a role for GM₁-gangliosides in transmembrane signalling and in the mechanism of action of cholera toxin.

Original language	English
Pages (from-to)	1216-1222
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	102
Issue number	4
DOIs	https://doi.org/10.1016/S0006-291X(81)80141-6
State	Published - Oct 30 1981

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(81)80141-6

Cite this

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title = "Cytoskeletal association of the cholera toxin receptor in rat erythrocytes",

abstract = "Cholera toxin receptors are associated with the cytoskeletal residue of Triton X-100 extracts of rat erythrocytes. The solubilized cytoskeletal toxin-receptor complex appears to be a large macromolecular entity whose formation is facilitated by increased receptor occupancy. These findings suggest a role for GM1-gangliosides in transmembrane signalling and in the mechanism of action of cholera toxin.",

author = "Naji Sahyoun and Talal Shatila and Harry Levine and Pedro Cuatrecasas",

year = "1981",

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doi = "10.1016/S0006-291X(81)80141-6",

language = "English",

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T1 - Cytoskeletal association of the cholera toxin receptor in rat erythrocytes

AU - Sahyoun, Naji

AU - Shatila, Talal

AU - Levine, Harry

AU - Cuatrecasas, Pedro

PY - 1981/10/30

Y1 - 1981/10/30

N2 - Cholera toxin receptors are associated with the cytoskeletal residue of Triton X-100 extracts of rat erythrocytes. The solubilized cytoskeletal toxin-receptor complex appears to be a large macromolecular entity whose formation is facilitated by increased receptor occupancy. These findings suggest a role for GM1-gangliosides in transmembrane signalling and in the mechanism of action of cholera toxin.

AB - Cholera toxin receptors are associated with the cytoskeletal residue of Triton X-100 extracts of rat erythrocytes. The solubilized cytoskeletal toxin-receptor complex appears to be a large macromolecular entity whose formation is facilitated by increased receptor occupancy. These findings suggest a role for GM1-gangliosides in transmembrane signalling and in the mechanism of action of cholera toxin.

UR - https://www.scopus.com/pages/publications/0019869844

UR - https://www.scopus.com/pages/publications/0019869844#tab=citedBy

U2 - 10.1016/S0006-291X(81)80141-6

DO - 10.1016/S0006-291X(81)80141-6

M3 - Article

C2 - 7198441

AN - SCOPUS:0019869844

SN - 0006-291X

VL - 102

SP - 1216

EP - 1222

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Cytoskeletal association of the cholera toxin receptor in rat erythrocytes

Abstract

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