共 71 条
Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER
被引:181
作者:

Chinnapen, Daniel J. -F.
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机构: Harvard Univ, Childrens Hosp Boston, Ctr Digest Dis, GI Cell Biol, Boston, MA 02115 USA

Chinnapen, Himani
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机构: Harvard Univ, Childrens Hosp Boston, Ctr Digest Dis, GI Cell Biol, Boston, MA 02115 USA

Saslowsky, David
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机构: Harvard Univ, Childrens Hosp Boston, Ctr Digest Dis, GI Cell Biol, Boston, MA 02115 USA

Lencer, Wayne I.
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机构: Harvard Univ, Childrens Hosp Boston, Ctr Digest Dis, GI Cell Biol, Boston, MA 02115 USA
机构:
[1] Harvard Univ, Childrens Hosp Boston, Ctr Digest Dis, GI Cell Biol, Boston, MA 02115 USA
[2] Harvard Univ, Sch Med, Dept Pediat, Boston, MA 02115 USA
[3] Harvard Univ, Ctr Digest Dis, Boston, MA 02115 USA
关键词:
cholera toxin;
lipid raft;
retrograde pathway;
GM1;
AB(5) toxin;
endocytosis;
D O I:
10.1111/j.1574-6968.2006.00545.x
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
Cholera toxin (CT), and members of the AB(5) family of toxins enter host cells and hijack the cell's endogenous pathways to induce toxicity. CT binds to a lipid receptor on the plasma membrane (PM), ganglioside GM1, which has the ability to associate with lipid rafts. The toxin can then enter the cell by various modes of receptor-mediated endocytosis and traffic in a retrograde manner from the PM to the Golgi and the endoplasmic reticulum (ER). Once in the ER, a portion of the toxin is unfolded and retro-translocated to the cytosol so as to induce disease. GM1 is the vehicle that carries CT from PM to ER. Thus, the toxin pathway from PM to ER is a lipid-based sorting pathway, which is potentially meditated by the determinants of the GM1 ganglioside structure itself.
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页码:129 / 137
页数:9
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