|
Originally published In Press as doi:10.1074/jbc.M008062200 on November 1, 2000
J. Biol. Chem., Vol. 276, Issue 5, 3384-3393, February 2, 2001
Targeting of Membrane Proteins to the Regulated Secretory Pathway
in Anterior Pituitary Endocrine Cells*
Rajaâ
El Meskini,
Gregory J.
Galano,
Ruth
Marx,
Richard E.
Mains, and
Betty A.
Eipper
From the Department of Neuroscience, University of Connecticut
Health Center, Farmington, Connecticut 06030-3401
Unlike the neuroendocrine cell lines widely used
to study trafficking of soluble and membrane proteins to secretory
granules, the endocrine cells of the anterior pituitary are highly
specialized for the production of mature secretory granules. Therefore,
we investigated the trafficking of three membrane proteins in primary anterior pituitary endocrine cells. Peptidylglycine -amidating monooxygenase (PAM), an integral membrane protein essential to the production of many bioactive peptides, is cleaved and enters the
regulated secretory pathway even when expressed at levels 40-fold
higher than endogenous levels. Myc-TMD/CD, a membrane protein lacking
the lumenal, catalytic domains of PAM, is still stored in granules.
Secretory granules are not the default pathway for all membrane
proteins, because Tac accumulates on the surface of pituitary endocrine
cells. Overexpression of PAM is accompanied by a diminution in its
endoproteolytic cleavage and in its BaCl2-stimulated release from mature granules. Because internalized PAM/PAM-antibody complexes are returned to secretory granules, the endocytic machinery of the pituitary endocrine cells is not saturated. As in corticotrope tumor cells, expression of PAM or Myc-TMD/CD alters the organization of
the actin cytoskeleton. PAM-mediated alterations in the cytoskeleton may limit maturation of PAM and storage in mature granules.
*
This work was supported by National Institutes of Health
Grant DK-32949.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Neuroscience,
University of Connecticut Health Center, 263 Farmington Ave.,
Farmington, CT 06030-3401. Tel.: 860-679-8898; Fax:
860-679-1885; E-mail: eipper@uchc.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
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]
|
 |
|

|
 |

|
 |
 
F. Ferraro, B. A. Eipper, and R. E. Mains
Retrieval and Reuse of Pituitary Secretory Granule Proteins
J. Biol. Chem.,
July 8, 2005;
280(27):
25424 - 25435.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
X. Xin, F. Ferraro, N. Back, B. A. Eipper, and R. E. Mains
Cdk5 and Trio modulate endocrine cell exocytosis
J. Cell Sci.,
September 15, 2004;
117(20):
4739 - 4748.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
R. El Meskini, V. C. Culotta, R. E. Mains, and B. A. Eipper
Supplying Copper to the Cuproenzyme Peptidylglycine alpha -Amidating Monooxygenase
J. Biol. Chem.,
March 28, 2003;
278(14):
12278 - 12284.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
T. C. Steveson, G. D. Ciccotosto, X.-M. Ma, G. P. Mueller, R. E. Mains, and B. A. Eipper
Menkes Protein Contributes to the Function of Peptidylglycine {alpha}-Amidating Monooxygenase
Endocrinology,
January 1, 2003;
144(1):
188 - 200.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. B. Scott, T. A. Blanpied, G. T. Swanson, C. Zhang, and M. D. Ehlers
An NMDA Receptor ER Retention Signal Regulated by Phosphorylation and Alternative Splicing
J. Neurosci.,
May 1, 2001;
21(9):
3063 - 3072.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
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]
|
 |
|
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|