Export of Cellubrevin from the Endoplasmic Reticulum Is Controlled by BAP31

@article{Annaert1997ExportOC,
  title={Export of Cellubrevin from the Endoplasmic Reticulum Is Controlled by BAP31 },
  author={Wim Annaert and Bernd Becker and Ute Kistner and Michael Reth and Reinhard Jahn},
  journal={The Journal of Cell Biology},
  year={1997},
  volume={139},
  pages={1397 - 1410}
}
Cellubrevin is a ubiquitously expressed membrane protein that is localized to endosomes throughout the endocytotic pathway and functions in constitutive exocytosis. We report that cellubrevin binds with high specificity to BAP31, a representative of a highly conserved family of integral membrane proteins that has recently been discovered to be binding proteins of membrane immunoglobulins. The interaction between BAP31 and cellubrevin is sensitive to high ionic strength and appears to require… CONTINUE READING
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