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Papers In Press, published online ahead of print June 6, 2001
J. Biol. Chem, 10.1074/jbc.M103936200
Submitted on May 2, 2001
Revised on June 3, 2001
Accepted on June 4, 2001

Response of an integral granule membrane protein to changes in pH

L. Chastine Bell-Parikh, Betty A. Eipper, and Richard E. Mains

Neuroscience, The University of Connecticut Health Center, Farmington, CT 06030-3401

Corresponding Author: mains{at}uchc.edu

A key feature of the regulated secretory pathway in neuroendocrine cells is lumenal pH, which decreases between trans-Golgi network and mature secretory granules. Since Peptidylglycine a-Amidating Monooxygenase (PAM) is one of the few membrane-spanning proteins concentrated in secretory granules and is a known effector of regulated secretion, we examined its sensitivity to pH. Based on antibody binding experiments, the non-catalytic linker regions between the two enzymatic domains of PAM show pH dependent conformational changes; these changes occur in the presence or absence of a transmembrane domain. Integral membrane PAM-1 solubilized from rat anterior pituitary or from transfected AtT-20 cells aggregates reversibly at pH 5.5 while retaining enzyme activity. Over 35% of the PAM-1 in anterior pituitary extracts aggregates at pH 5.5, while only about 5% aggregates at pH 7.5. PAM-1 recovered from secretory granules and endosomes is highly responsive to low pH-induced aggregation while PAM-1 recovered from a light, intracellular recycling compartment is not. Mutagenesis studies indicate that a transmembrane domain is necessary, but not sufficient for low pH-induced aggregation and reveal a short lumenal, juxtamembrane segment that also contributes to pH-dependent aggregation. Taken together, these results demonstrate that several properties of membrane PAM serve as indicators of granule pH in neuroendocrine cells.


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