Oligomeric Dop1p is Part of the Endosomal Neo1p-Ysl2p-Arl1p Membrane Remodeling Complex
| Autor: | Dagmar Pratte, Rüdiger Pipkorn, Sónia Barbosa, Heinz Schwarz, Birgit Singer-Krüger |
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| Rok vydání: | 2010 |
| Předmět: |
Scaffold protein
Saccharomyces cerevisiae Proteins Endosome Recombinant Fusion Proteins Vesicular Transport Proteins Endosomes Saccharomyces cerevisiae Biochemistry Clathrin Cell membrane Structural Biology Gene Expression Regulation Fungal Genetics medicine Phospholipid Transfer Proteins Molecular Biology Monomeric GTP-Binding Proteins Adenosine Triphosphatases biology Membrane transport protein Cell Membrane Membrane Transport Proteins Signal transducing adaptor protein Intracellular Membranes Cell Biology Flippase Membrane budding Cell biology medicine.anatomical_structure Multiprotein Complexes Mutation biology.protein trans-Golgi Network |
| Zdroj: | Traffic. 11:1092-1106 |
| ISSN: | 1398-9219 |
| DOI: | 10.1111/j.1600-0854.2010.01079.x |
| Popis: | Yeast Dop1p is an essential protein that is highly conserved in evolution and whose function is largely unknown. Here, we provide evidence that Dop1p localizes to endosomes and exists in a complex with two other conserved proteins: Neo1p, a P(4)-ATPase and putative flippase, and the scaffolding protein Ysl2p/Mon2p. The latter operates during membrane budding at the tubular endosomal network/trans-Golgi network (TEN/TGN) in a process that includes clathrin recruitment via adaptor proteins. Consistent with a role for Dop1p during this process, temperature-sensitive dop1-3 cells accumulate multivesicular, elongated tubular and ring-like structures similar to those displayed by neo1 and ysl2 mutants. In further agreement with the concept of Dop1p-Neo1p-Ysl2p complex formation and co-operation, we show that dop1-3 cells exhibit reduced levels of Neo1p and Ysl2p at steady state. Conversely, mutations or deletions in NEO1 and YSL2 lead to a decrease in Dop1p levels. In addition to binding to Neo1p and Ysl2p, Dop1p can form dimers or multimers. A critical region for dimerization resides in the C-terminus with leucine zipper-like domains. Dop1p's membrane association is largely mediated by its internal region, but Ysl2p might not be crucial for membrane recruitment. |
| Databáze: | OpenAIRE |
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