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J. Biol. Chem., Vol. 276, Issue 30, 27881-27892, July 27, 2001

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Addition of a Glycophosphatidylinositol to Acetylcholinesterase
PROCESSING, DEGRADATION, AND SECRETION^*

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

From the Laboratoire de Neurobiologie Moléculaire et Cellulaire, CNRS UMR 8544, Ecole Normale Supérieure, 46 rue d'Ulm, 75005 Paris, France

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 / + 1/ + 2, particularly   1. 5) Glypiation was not affected by the closeness of the  site to the ₁₀ helix of the catalytic domain. 6) A cysteine could simultaneously form a disulfide bond and serve as an  site; however, there was a mutual interference between glypiation and the formation of an intercatenary disulfide bond, at a short distance upstream of . 7) Glypiation was not affected by the presence of an N-glycosylation site at  or in its vicinity or by the addition of a short hydrophilic, highly charged peptide (FLAG; DYKDDDDK) at the C terminus of the hydrophobic region.

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