Deficiencies in the Endoplasmic Reticulum (ER)-Membrane Protein Gab1p Perturb Transfer of Glycosylphosphatidylinositol to Proteins and Cause Perinuclear ER-associated Actin Bar Formation
| العنوان: | Deficiencies in the Endoplasmic Reticulum (ER)-Membrane Protein Gab1p Perturb Transfer of Glycosylphosphatidylinositol to Proteins and Cause Perinuclear ER-associated Actin Bar Formation |
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| المؤلفون: | Peter Orlean, Erfei Bi, Serguei E. Tcheperegine, Xiang Dong Gao, Anne Farewell, Kathleen Corrado, Paul S. Martin, Stephen J. Grimme, Kimberly C. Tu |
| المصدر: | Molecular Biology of the Cell. 15:2758-2770 |
| بيانات النشر: | American Society for Cell Biology (ASCB), 2004. |
| سنة النشر: | 2004 |
| مصطلحات موضوعية: | Saccharomyces cerevisiae Proteins, Glycosylphosphatidylinositols, Protein subunit, Molecular Sequence Data, GAB1, Saccharomyces cerevisiae, Biology, Endoplasmic Reticulum, Cell membrane, medicine, Amino Acid Sequence, Cloning, Molecular, Molecular Biology, Alleles, Conserved Sequence, Actin, Genes, Essential, Endoplasmic reticulum, Cell Membrane, Cell Polarity, Membrane Proteins, Articles, Cell Biology, Actin cytoskeleton, Molecular biology, Actins, Cell biology, Transport protein, Protein Subunits, Protein Transport, medicine.anatomical_structure, Membrane protein, Sequence Alignment, Acyltransferases, Gene Deletion, Protein Binding |
| الوصف: | The essential GAB1 gene, which encodes an endoplasmic reticulum (ER)-membrane protein, was identified in a screen for mutants defective in cellular morphogenesis. A temperature-sensitive gab1 mutant accumulates complete glycosylphosphatidylinositol (GPI) precursors, and its temperature sensitivity is suppressed differentially by overexpression of different subunits of the GPI transamidase, from strong suppression by Gpi8p and Gpi17p, to weak suppression by Gaa1p, and to no suppression by Gpi16p. In addition, both Gab1p and Gpi17p localize to the ER and are in the same protein complex in vivo. These findings suggest that Gab1p is a subunit of the GPI transamidase with distinct relationships to other subunits in the same complex. We also show that depletion of Gab1p or Gpi8p, but not Gpi17p, Gpi16p, or Gaa1p causes accumulation of cofilin-decorated actin bars that are closely associated with the perinuclear ER, which highlights a functional interaction between the ER network and the actin cytoskeleton. |
| تدمد: | 1939-4586 1059-1524 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9b289d02d76a6f7647c719945f4f5da https://doi.org/10.1091/mbc.e04-01-0035 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....e9b289d02d76a6f7647c719945f4f5da |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19394586 10591524 |
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