JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on July 20, 2001
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
276/30/27881    most recent
M010817200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Coussen, F.
Right arrow Articles by Bon, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Coussen, F.
Right arrow Articles by Bon, S.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print May 3, 2001
J. Biol. Chem, 10.1074/jbc.M010817200
Submitted on November 30, 2000
Revised on May 1, 2001
Accepted on May 3, 2001

Addition of a glycophosphatidylinositol (GPI) to acetylcholinesterase: processing, degradation and secretion

Françoise Coussen, Annick Ayon, Anne Le Goff, Jacqueline Leroy, Jean Massoulié, and Suzanne Bon

Laboratoire de Neurobiologie Cellulaire et Moléculaire, CNRS UMR 8544, Paris 75005

Corresponding Author: jean.massoulie{at}biologie.ens.fr

We introduced various mutations and modifications in the GPI anchoring signal of rat acetylcholinesterase (AChE). 1] The resulting mutants, expressed in transiently transfected COS cells, were initially produced at the same rate, in an active form, but the fraction of GPI-anchored AChE and the steady state level of AChE activity varied over a wide range. 2] Productive interaction with the GPI addition machinery led to GPI-anchoring, secretion of uncleaved protein and secretion of a cleaved protein, in variable proportions; unproductive interaction led to degradation: poorly processed molecules were degraded rather than retained intracellularly or secreted. 3] An efficient glypiation appeared necessary, but not sufficient for a high level of secretion; the cleaved, secreted protein was possibly generated as a by-product of transamidation. 4] Glypiation was influenced by a wider context than the triplet w/w+1/w+2, particularly w-1. 5] Glypiation was not affected by the closeness of the w site to the a10 helix of the catalytic domain. 6] A cysteine could simultaneously form a disulfide bond and serve as an w site; however, there was a mutual interference between glypiation and the formation of an intercatenary disulfide bond, at a short distance upstream of w. 7] Glypiation was not affected by the presence of an N-glycosylation site at w or in its vicinity, or by addition of a short hydrophilic, highly charged peptide ("FLAG": DYKDDDDK) at the C-terminus of the hydrophobic region.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Am. J. Physiol. Cell Physiol.Home page
G. M. Verghese, M. F. Gutknecht, and G. H. Caughey
Prostasin regulates epithelial monolayer function: cell-specific Gpld1-mediated secretion and functional role for GPI anchor
Am J Physiol Cell Physiol, December 1, 2006; 291(6): C1258 - C1270.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Falasca, N. Perrier, J. Massoulie, and S. Bon
Determinants of the t Peptide Involved in Folding, Degradation, and Secretion of Acetylcholinesterase
J. Biol. Chem., January 14, 2005; 280(2): 878 - 886.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
F. Naghibalhossaini and C. P. Stanners
Minimal mutations are required to effect a radical change in function in CEA family members of the Ig superfamily
J. Cell Sci., February 15, 2004; 117(5): 761 - 769.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
B. Eisenhaber, M. Wildpaner, C. J. Schultz, G. H.H. Borner, P. Dupree, and F. Eisenhaber
Glycosylphosphatidylinositol Lipid Anchoring of Plant Proteins. Sensitive Prediction from Sequence- and Genome-Wide Studies for Arabidopsis and Rice
Plant Physiology, December 1, 2003; 133(4): 1691 - 1701.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
G. H.H. Borner, D. J. Sherrier, T. J. Stevens, I. T. Arkin, and P. Dupree
Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis
Plant Physiology, June 1, 2002; 129(2): 486 - 499.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Morel, J. Leroy, A. Ayon, J. Massoulie, and S. Bon
Acetylcholinesterase H and T Dimers Are Associated through the Same Contact. MUTATIONS AT THIS INTERFACE INTERFERE WITH THE C-TERMINAL T PEPTIDE, INDUCING DEGRADATION RATHER THAN SECRETION
J. Biol. Chem., September 28, 2001; 276(40): 37379 - 37389.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.