The brefeldin A-inhibited guanine nucleotide-exchange protein, BIG2, regulates the constitutive release of TNFR1 exosome-like vesicles.

@article{Islam2007TheBA,
  title={The brefeldin A-inhibited guanine nucleotide-exchange protein, BIG2, regulates the constitutive release of TNFR1 exosome-like vesicles.},
  author={Aminul Islam and Xiaoyan Shen and Toyoko Hiroi and Joel Moss and Martha Vaughan and Stewart J. Levine},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 13},
  pages={9591-9}
}
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… CONTINUE READING
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