Three members of the yeast N-BAR proteins family form heterogeneous lattices in vivo and interact differentially with two RabGAP proteins
| Autor: | Hélène Tisserand, Marie-Hélène Cuif, Magali Prigent, Julien Chaillot, Emmanuelle Boy-Marcotte |
|---|---|
| Přispěvatelé: | Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Autophagie et Développement (OTOFAJ), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins GTPase-activating protein Immunoprecipitation [SDV]Life Sciences [q-bio] lcsh:Medicine Membrane curvature Saccharomyces cerevisiae Article Exocytosis 03 medical and health sciences Bimolecular fluorescence complementation 0302 clinical medicine Organelle lcsh:Science Cytoskeleton Multidisciplinary Chemistry lcsh:R GTPase-Activating Proteins Microfilament Proteins Endocytosis Yeast Cell biology 030104 developmental biology Multiprotein Complexes Amphiphysin lcsh:Q Rab 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Scientific Reports Scientific Reports, Nature Publishing Group, 2020, 10 (1), pp.1698. ⟨10.1038/s41598-020-58606-2⟩ Scientific Reports, 2020, 10 (1), pp.1698. ⟨10.1038/s41598-020-58606-2⟩ Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020) |
| ISSN: | 2045-2322 |
| Popis: | The yeast N-BAR (Bin/Amphiphysin/Rvs167) protein Rvs167 is recruited by the Rab GTPase Activating Proteins (RabGAP) Gyp5 and Gyl1 to the tip of small buds to act in exocytosis. Investigating other N-BAR proteins involved in Gyp5/Gyl1/Rvs167 complexes, we found that Rvs161, an Rvs167 paralog, is absent from the complexes formed at the tip of small buds. Immunoprecipitation and Bimolecular Fluorescence Complementation (BiFC) analysis show that both Rvs167 and Rvs161 interact in vivo with Gvp36, an N-BAR protein. Rvs167 molecules also interact independently of Rvs161 and Gvp36. Rvs167/Rvs167 and Rvs167/Gyp5 interactions predominate over other combinations at the tip of small buds, suggesting that N-BAR lattices enriched in Rvs167 molecules form at these sites. By combining BiFC with markers specific to each organelle, we analyzed systematically in living cells the locations of the BiFC signals generated by combinations of the three N-BAR proteins. We show that the BiFC signals differ according to organelle and cell site, strongly suggesting heterogeneity in the composition of N-BAR protein lattices in vivo. Our results reveal that the organization of N-BAR protein lattices in vivo is complex and are consistent with N-BAR proteins forming various types of dimers and lattices of variable composition. |
| Databáze: | OpenAIRE |
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