[HTML][HTML] The brefeldin A-inhibited guanine nucleotide-exchange protein, BIG2, regulates the constitutive release of TNFR1 exosome-like vesicles
A Islam, X Shen, T Hiroi, J Moss, M Vaughan… - Journal of biological …, 2007 - ASBMB
The type I, 55-kDa tumor necrosis factor receptor (TNFR1) is released from cells to the
extracellular space where it can bind and modulate TNF bioactivity. Extracellular TNFR1
release occurs by two distinct pathways: the inducible proteolytic cleavage of TNFR1
ectodomains and the constitutive release of full-length TNFR1 in exosome-like vesicles.
Regulation of both TNFR1 release pathways appears to involve the trafficking of cytoplasmic
TNFR1 vesicles. Vesicular trafficking is controlled by ADP-ribosylation factors (ARFs), which …
extracellular space where it can bind and modulate TNF bioactivity. Extracellular TNFR1
release occurs by two distinct pathways: the inducible proteolytic cleavage of TNFR1
ectodomains and the constitutive release of full-length TNFR1 in exosome-like vesicles.
Regulation of both TNFR1 release pathways appears to involve the trafficking of cytoplasmic
TNFR1 vesicles. Vesicular trafficking is controlled by ADP-ribosylation factors (ARFs), which …
