XLαs is a new type of G protein
RH Kehlenbach, J Matthey, WB Huttner - Nature, 1994 - nature.com
RH Kehlenbach, J Matthey, WB Huttner
Nature, 1994•nature.comThe GTP-binding proteins are well-known regulators of cellular functions1–4, including
vesicular transport5–7. Cholera toxin, which is known to catalyse ADP-ribosylation of the as
subunit of hetero-trimeric G proteins, stimulates secretory vesicle formation from the trans-
Golgi network8. Here we describe a new cholera toxin target, an'extra large'G protein (XLαs;
Mr 92K) which consists of a new 51K XL-portion linked to a Gαs truncated at the amino
terminus. XLαs is specifically associated with the trans-Golgi net-work and occurs selectively …
vesicular transport5–7. Cholera toxin, which is known to catalyse ADP-ribosylation of the as
subunit of hetero-trimeric G proteins, stimulates secretory vesicle formation from the trans-
Golgi network8. Here we describe a new cholera toxin target, an'extra large'G protein (XLαs;
Mr 92K) which consists of a new 51K XL-portion linked to a Gαs truncated at the amino
terminus. XLαs is specifically associated with the trans-Golgi net-work and occurs selectively …
Abstract
THE GTP-binding proteins are well-known regulators of cellular functions1–4, including vesicular transport5–7. Cholera toxin, which is known to catalyse ADP-ribosylation of the as subunit of hetero-trimeric G proteins, stimulates secretory vesicle formation from the trans-Golgi network8. Here we describe a new cholera toxin target, an 'extra large' G protein (XLαs; Mr 92K) which consists of a new 51K XL-portion linked to a Gαs truncated at the amino terminus. XLαs is specifically associated with the trans-Golgi net-work and occurs selectively in cells containing both the regulated and the constitutive pathway of protein secretion. Hence, XLαs may mediate the effects of cholera toxin on secretory vesicle formation.
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