Tracking exocytosis of a GPI-anchored protein in Aspergillus nidulans
العنوان: | Tracking exocytosis of a GPI-anchored protein in Aspergillus nidulans |
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المؤلفون: | Miguel A. Peñalva, Esteban Moscoso-Romero, Miguel Hernandez-Gonzalez |
المساهمون: | Ministerio de Ciencia e Innovación (España), Comunidad de Madrid, Peñalva, Miguel Ángel [0000-0002-3102-2806], Moscoso, Esteban [0000-0003-3755-7366], Hernández-González, Miguel [0000-0001-7445-314X], Peñalva, Miguel Ángel, Moscoso, Esteban, Hernández-González, Miguel |
المصدر: | Digital.CSIC. Repositorio Institucional del CSIC instname |
بيانات النشر: | John Wiley & Sons, 2020. |
سنة النشر: | 2020 |
مصطلحات موضوعية: | Glycosylphosphatidylinositols, Endosome, Golgi Apparatus, Glycosylphosphatidylinositol anchor, Biology, Endoplasmic Reticulum, Biochemistry, Aspergillus nidulans, Exocytosis, 03 medical and health sciences, symbols.namesake, 0302 clinical medicine, Structural Biology, Genetics, Secretion, Molecular Biology, COPII, Secretory pathway, 030304 developmental biology, 0303 health sciences, GPI remodeling, Secretory Pathway, Endoplasmic reticulum, Trans-Golgi network (TGN), Cell Biology, Golgi apparatus, Cell biology, Protein Transport, Intracellular traffic, symbols, RAB11, 030217 neurology & neurosurgery, Biogenesis |
الوصف: | 39 p.-9 fig. Secretion of the GPI‐anchored protein (GPI‐AP) EglC was investigated in the filamentous fungus Aspergillus nidulans, exploiting a sucrose‐inducible promoter to conditionally express the protein in cells blocked at different steps of exocytosis. EglC is delivered to the cell surface in a polarized fashion, but appears to redistribute rapidly towards apico‐distal regions. Inactivation of SarASar1 mediating COPII vesicle biogenesis resulted in the accumulation of EglC in the ER but, rather than concentrating in ER‐exit‐sites, the reporter labeled the ER uniformly. Abnormal posttranslational modifications of EglC were detected in sarAts and sed5ts mutants, suggesting that blocking COPII biogenesis or traffic in the ER/Golgi interface might affect GPI remodeling. EglC delivery to the PM requires, besides Golgi function, the TRAPPII complex mediating the biogenesis of RAB11 secretory vesicles at the TGN, but is unaffected by the absence of RAB5, the key regulator of early endosome biogenesis/maturation. Thus, unlike the soluble extracellular enzyme inulinase, EglC is directly delivered from the TGN to the plasma membrane without involvement of endosomes. We conclude that in A. nidulans GPI‐APs follow a direct secretory pathway from the ER to the plasma membrane. Work supported by Agencia Española de Investigación Grants BIO2015-65090-R and RTI2018-093344-B100 and by the Comunidad de Madrid Grant B2017/BMD-3691 “InGEMICS-CM” (with contributions of the European Social Fund and the European Regional Development Fund), to MAP. |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9824df37c8989005d01ff4dc6135a85Test http://hdl.handle.net/10261/219959Test |
حقوق: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....d9824df37c8989005d01ff4dc6135a85 |
قاعدة البيانات: | OpenAIRE |
الوصف غير متاح. |