Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme.

@article{Alam1996NovelPT,
  title={Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme.},
  author={M d Rowshon Alam and Benjamin D Caldwell and Re-reading Chalmers Johnson and Daniel N. Darlington and Richard E Mains and Betty A Eipper},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 45},
  pages={28636-40}
}
The steady state distribution of membrane forms of peptidylglycine alpha-amidating monooxygenase (PAM) in the secretory pathway of neurons and endocrine cells depends on signals in its cytosolic COOH-terminal domain (CD). Mutagenesis studies yielded catalytically active PAM proteins that are not properly localized or internalized. Employing the yeast two-hybrid system, we isolated two distinct cDNAs whose protein products showed a strong interaction with the CD of PAM. The interaction of these… CONTINUE READING

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