JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rindler, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rindler, M. J.

J Biol Chem, Vol. 273, Issue 47, 31180-31185, November 20, 1998

Carboxypeptidase E, a Peripheral Membrane Protein Implicated in the Targeting of Hormones to Secretory Granules, Co-aggregates with Granule Content Proteins at Acidic pH

Michael J. Rindler

From the Department of Cell Biology and Kaplan Cancer Center, New York University Medical Center, New York, New York 10016

Carboxypeptidase E (CPE) is a prohormone-processing enzyme and peripheral membrane protein of endocrine/neuroendocrine secretory granules. CPE has been shown to bind to an amino-terminal peptide of pro-opiomelanocortin (N-POMC) at pH 5.5 and hypothesized to be critically involved in the targeting of hormones such as POMC to the regulated secretory pathway [Cool, D. R., Normant, E., Shen, F., Chen, H. C., Pannell, L., Zhang, Y., and Loh, Y. P. (1997) Cell 88, 73-83]. To further explore the possibility that CPE serves to mediate the association of content proteins with the membrane during granule biogenesis, the binding of CPE to granule content proteins was investigated using an in vitro aggregation assay in which the selective precipitation of granule content proteins is induced by titration of the pH to <6.0. CPE was observed to co-aggregate efficiently with pituitary and chromaffin granule content proteins at concentrations well below those that promote its self-aggregation. In addition, CPE co-precipitated at pH 5.8 with purified prolactin and with insulin, which homophillically self-aggregate yet are structurally distinct from N-POMC. N-POMC when added to the assays did not inhibit the aggregation of CPE with prolactin or insulin, indicating that these interactions do not involve a binding site for N-POMC. The data show that CPE interacts at acidic pH with a variety of different content proteins, resembling in this regard other granule membrane proteins. The results support the idea that co-aggregation of abundant membrane proteins with content proteins is an important general mechanism for the sorting and retention of secretory granule proteins during granule maturation.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
Y. Brunner, Y. Coute, M. Iezzi, M. Foti, M. Fukuda, D. F. Hochstrasser, C. B. Wollheim, and J.-C. Sanchez
Proteomics Analysis of Insulin Secretory Granules
Mol. Cell. Proteomics, June 1, 2007; 6(6): 1007 - 1017.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
J. A. Sobota, F. Ferraro, N. Back, B. A. Eipper, and R. E. Mains
Not All Secretory Granules Are Created Equal: Partitioning of Soluble Content Proteins
Mol. Biol. Cell, December 1, 2006; 17(12): 5038 - 5052.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
S. G. Venkatesh, D. J Cowley, and S.-U. Gorr
Differential aggregation properties of secretory proteins that are stored in exocrine secretory granules of the pancreas and parotid glands
Am J Physiol Cell Physiol, February 1, 2004; 286(2): C365 - C371.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
M. Hosaka, M. Suda, Y. Sakai, T. Izumi, T. Watanabe, and T. Takeuchi
Secretogranin III Binds to Cholesterol in the Secretory Granule Membrane as an Adapter for Chromogranin A
J. Biol. Chem., January 30, 2004; 279(5): 3627 - 3634.
[Abstract] [Full Text] [PDF]

Home page
 Ann. N. Y. Acad. Sci.Home page
Y. P. LOH, A. MALDONADO, C. ZHANG, W. H. TAM, and N. CAWLEY
Mechanism of Sorting Proopiomelanocortin and Proenkephalin to the Regulated Secretory Pathway of Neuroendocrine Cells
Ann. N.Y. Acad. Sci., October 1, 2002; 971(1): 416 - 425.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
A. D. Blagoveshchenskaya, M. J. Hannah, S. Allen, and D. F. Cutler
Selective and Signal-dependent Recruitment of Membrane Proteins to Secretory Granules Formed by Heterologously Expressed von Willebrand Factor
Mol. Biol. Cell, May 1, 2002; 13(5): 1582 - 1593.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
B.-J. Sankoorikal, Y. L. Zhu, M. E. Hodsdon, E. Lolis, and P. S. Dannies
Aggregation of Human Wild-Type and H27A-Prolactin in Cells and in Solution: Roles of Zn2+, Cu2+, and pH
Endocrinology, April 1, 2002; 143(4): 1302 - 1309.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
C. Zurzolo and C. Bowler
Exploring Bioinorganic Pattern Formation in Diatoms. A Story of Polarized Trafficking
Plant Physiology, December 1, 2001; 127(4): 1339 - 1345.
[Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. C. Steveson, G. C. Zhao, H. T. Keutmann, R. E. Mains, and B. A. Eipper
Access of a Membrane Protein to Secretory Granules Is Facilitated by Phosphorylation
J. Biol. Chem., October 19, 2001; 276(43): 40326 - 40337.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
R. Kuliawat, D. Prabakaran, and P. Arvan
Proinsulin Endoproteolysis Confers Enhanced Targeting of Processed Insulin to the Regulated Secretory Pathway
Mol. Biol. Cell, June 1, 2000; 11(6): 1959 - 1972.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
M. D. Turner and P. Arvan
Protein Traffic from the Secretory Pathway to the Endosomal System in Pancreatic beta -Cells
J. Biol. Chem., May 5, 2000; 275(19): 14025 - 14030.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
D. E. Krantz, C. Waites, V. Oorschot, Y. Liu, R. I. Wilson, P. K. Tan, J. Klumperman, and R. H. Edwards
A Phosphorylation Site Regulates Sorting of the Vesicular Acetylcholine Transporter to Dense Core Vesicles
J. Cell Biol., April 17, 2000; 149(2): 379 - 396.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. J. Cowley, Y. R. Moore, D. S. Darling, P. B. M. Joyce, and S.-U. Gorr
N- and C-terminal Domains Direct Cell Type-specific Sorting of Chromogranin A to Secretory Granules
J. Biol. Chem., March 10, 2000; 275(11): 7743 - 7748.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
S.-U. Gorr, X. F. Huang, D. J. Cowley, R. Kuliawat, and P. Arvan
Disruption of disulfide bonds exhibits differential effects on trafficking of regulated secretory proteins
Am J Physiol Cell Physiol, July 1, 1999; 277(1): C121 - C131.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. S. Lee, Y. L. Zhu, J. E. Chang, and P. S. Dannies
Acquisition of Lubrol Insolubility, a Common Step for Growth Hormone and Prolactin in the Secretory Pathway of Neuroendocrine Cells
J. Biol. Chem., January 5, 2001; 276(1): 715 - 721.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. C. Bell-Parikh, B. A. Eipper, and R. E. Mains
Response of an Integral Granule Membrane Protein to Changes in pH
J. Biol. Chem., August 3, 2001; 276(32): 29854 - 29863.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.