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Title: Capping of cholera toxin-ganglioside GM1 complexes on mouse lymphocytes is accompanied by co-capping of alpha-actinin.
Authors: Kellie, Stuart
Patel, Bipin
Pierce, Eric J.
Critchley, David R.
First Published: 1-Aug-1983
Publisher: Rockefeller University Press
Citation: The Journal of Cell Biology, 1983 vol. 97 no. 2 447-454
Abstract: We used cholera toxin, which binds exclusively and with a high affinity to the ganglioside GM1, as a probe to investigate the distribution of this glycolipid on the surface of mouse lymphocytes. When lymphocytes are incubated with cholera toxin (or its B subunit) and then sequentially with horse anti-toxin and FITC-swine anti-horse Ig at 37 degrees C, the cholera toxin-ganglioside GM1 complex is redistributed to a cap at one pole of the cell. The capping of cholera toxin-GM1 complexes is slower than the capping of surface-Ig complexes, requires two antibodies, and is inhibited at high toxin concentrations. Cholera toxin-GM1, like surface-Ig capping, is an energy-dependent process and is inhibited by sodium azide, low temperatures, or cytochalasin B, but is unaffected by demecolcine. An affinity-purified antibody against alpha-actinin was used to examine the distribution of this cytoskeletal component during the capping process. 88% of the cells that had a surface Ig cap displayed a co-cap of alpha-actinin, and 57% of the cells that had a cholera toxin-GM1 cap displayed a co-cap of alpha-actinin. Time course studies revealed similar kinetics of external ligand cap formation and the formation of alpha-actinin co-caps. We conclude that capping of a cell-surface glycolipid is associated with a reorganization of the underlying cytoskeleton. The implications of such an association are discussed in the context of current models of the mechanism of capping.
DOI Link: 10.1083/jcb.97.2.447
ISSN: 0021-9525
eISSN: 1540-8140
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported license as described at and
Appears in Collections:Published Articles, College of Medicine, Biological Sciences and Psychology

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