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The growth suppressing gas1 product is a GPI‐linked protein
Author(s) -
Stebel Marco,
Vatta Paolo,
Ruaro Maria Elisabetta,
Del Sal Giannino,
Parton Robert G.,
Schneider Claudio
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02004-4
Subject(s) - endoplasmic reticulum , immunoelectron microscopy , microbiology and biotechnology , phosphatidylinositol , signal peptide , target peptide , cleavage (geology) , chemistry , biology , signal transduction , peptide , antibody , peptide sequence , biochemistry , gene , paleontology , fracture (geology) , immunology
Growth arrest specific ( gas ) 1 gene product is expressed in non‐transformed fibroblasts in response to stimuli driving cells into Go phase. Gas1 has been demonstrated to inhibit cell proliferation when over‐expressed in proliferating fibroblasts. This activity depends on a function of the p53 protein independent of its transactivating ability. To better define the pathway leading from Gas1, which is located on the plasma membrane, to p53, we have undertaken a detailed characterization of its topology. We demonstrate that the protein undergoes cotranslational modifications in the endoplasmic reticulum, consisting of signal peptide cleavage, N‐linked glycosylation and glycosyl‐phosphatidylinositol anchor addition. Immunoelectron microscopy shows that, in its mature form, Gas1 is randomly distributed over the outer leaflet of the plasma membrane and that upon antibody‐induced clustering it relocalizes to caveolae.