ArticleGenetics1997
MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5.
Article in Genetics, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 69 citations in OpenAlex.
- Determinants of the cytosolic turnover of mitochondrial intermembrane space proteins.BMC biology · 2018Article
- Article
- Endocytic regulation of alkali metal transport proteins in mammals, yeast and plants.Current genetics · 2013Review
- Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants.PloS one · 2012Article
- A deubiquitylating complex required for neosynthesis of a yeast mitochondrial ATP synthase subunit.PloS one · 2012Article
- The endocytic adaptor proteins of pathogenic fungi: charting new and familiar pathways.Medical mycology · 2011Review
- Enhanced levels of Pis1p (phosphatidylinositol synthase) improve the growth of Saccharomyces cerevisiae cells deficient in Rsp5 ubiquitin ligase.The Biochemical journal · 2006Article
- Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2005Article
- Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S.Molecular biology of the cell · 2004Article
- Article
- Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2.Molecular and cellular biology · 2003Article
- Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast.Current genetics · 2003Article
- A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain.The EMBO journal · 2003Article
- Mathematical modeling of noise and discovery of genetic expression classes in gliomas.Oncogene · 2002Article
- Article
- Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae.Molecular and cellular biology · 2002Article
- Localization of the Rsp5p ubiquitin-protein ligase at multiple sites within the endocytic pathway.Molecular and cellular biology · 2001Article
- Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis.Molecular biology of the cell · 2001Article
- Article
- Ubiquitin is part of the retrovirus budding machinery.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alteration of the subcellular distribution of Mod5p-I, a tRNA modification enzyme, member of the sorting isozyme family, affects tRNA-mediated nonsense suppression. Altered suppression efficiency was used to identify MDP genes, which, when mutant, change the mitochondrial/cytosolic distribution of Mod5p-I,KR6. MDP2 is the previously identified VRP1, which encodes verprolin, required for proper organization of the actin cytoskeleton. MDP3 is identical to PAN1, which encodes a protein involved in initiation of translation and actin cytoskeleton organization. We report here the cloning and characterization of wild-type and mutant MDP1 alleles and the isolation and characterization of a multicopy suppressor of mdp1 mutations. MDP1 is identical to RSP5, which encodes ubiquitin-protein ligase, and mdp1 mutations are suppressed by high copy expression of ubiquitin. All four characterized mdp1 mutations cause missense changes located in the hect domain of Rsp5p that is highly conserved among ubiquitin-protein ligases. In addition to its well-known function in protein turnover, ubiquitination has been proposed to play roles in subcellular sorting of proteins via endocytosis and in delivery of proteins to peroxisomes, the endoplasmic reticulum and mitochondria. mdp1, as well as mdp2/vrp1 and mdp3/pan1 mutations, affect endocytosis. Further, mdp1 mutations show synthetic interactions with mdp2/vrp1 and mdp3/pan1. Identification of MDP1 as RSP5, along with our previous identification of MDP2/VRP1 and MDP3/PAN1, implicate interactions of the ubiquitin system, the actin cytoskeleton and protein synthesis in the subcellular distribution of proteins.
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