The endocytic pathways of a secretory granule membrane protein in HEK293 cells: PAM and EGF traverse a dynamic multivesicular body network together.

@article{Bck2017TheEP,
  title={The endocytic pathways of a secretory granule membrane protein in HEK293 cells: PAM and EGF traverse a dynamic multivesicular body network together.},
  author={Nils B{\"a}ck and Kristiina Kanerva and Vishwanatha Kurutihalli and Andrew Yanik and Elina Ikonen and Richard E Mains and Betty A Eipper},
  journal={European journal of cell biology},
  year={2017},
  volume={96 5},
  pages={
          407-417
        }
}
Peptidylglycine α-amidating monooxygenase (PAM) is highly expressed in neurons and endocrine cells, where it catalyzes one of the final steps in the biosynthesis of bioactive peptides. PAM is also expressed in unicellular organisms such as Chlamydomonas reinhardtii, which do not store peptides in secretory granules. As for other granule membrane proteins, PAM is retrieved from the cell surface and returned to the trans-Golgi network. This pathway involves regulated entry of PAM into… CONTINUE READING
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