ArticleG3 (Bethesda, Md.)2012
Genetic analysis of Mps3 SUN domain mutants in Saccharomyces cerevisiae reveals an interaction with the SUN-like protein Slp1.
Article in G3 (Bethesda, Md.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- A membrane-sensing mechanism links lipid metabolism to protein degradation at the nuclear envelope.The Journal of cell biology · 2023Article
- In Depth Topological Analysis of Arabidopsis Mid-SUN Proteins and Their Interaction with the Membrane-Bound Transcription Factor MaMYB.Plants (Basel, Switzerland) · 2023Article
- A progeroid syndrome caused by a deep intronic variant in TAPT1 is revealed by RNA/SI-NET sequencing.EMBO molecular medicine · 2023Article
- POD1-SUN-CRT3 chaperone complex guards the ER sorting of LRR receptor kinases in Arabidopsis.Nature communications · 2022Article
- Evolution and Functional Divergence ofFrontiers in plant science · 2021Article
- SUNny Ways: The Role of the SUN-Domain Protein Mps3 Bridging Yeast Nuclear Organization and Lipid Homeostasis.Frontiers in genetics · 2020Review
- Measuring similarity between gene interaction profiles.BMC bioinformatics · 2019Article
- Distribution of Proteins at the Inner Nuclear Membrane Is Regulated by the Asi1 E3 Ligase inGenetics · 2019Article
- Cell biology of yeast zygotes, from genesis to budding.Biochimica et biophysica acta · 2015Review
- Absence of SUN-domain protein Slp1 blocks karyogamy and switches meiotic recombination and synapsis from homologs to sister chromatids.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The plant LINC complex at the nuclear envelope.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2014Review
- Membrane-associated proteomics of chickpea identifies Sad1/UNC-84 protein (CaSUN1), a novel component of dehydration signaling.Scientific reports · 2014Article
- Protein interactions at the higher plant nuclear envelope: evidence for a linker of nucleoskeleton and cytoskeleton complex.Frontiers in plant science · 2014Review
- Requirement of the spindle pole body for targeting and/or tethering proteins to the inner nuclear membrane.Nucleus (Austin, Tex.)Article
- SUNrises on the International Plant Nucleus Consortium: SEB Salzburg 2012.Nucleus (Austin, Tex.)Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In virtually all eukaryotic cells, protein bridges formed by the conserved inner nuclear membrane SUN (for Sad1-UNC-84) domain-containing proteins and their outer nuclear membrane binding partners span the nuclear envelope (NE) to connect the nucleoplasm and cytoplasm. These linkages are important for chromosome movements within the nucleus during meiotic prophase and are essential for nuclear migration and centrosome attachment to the NE. In Saccharomyces cerevisiae, MPS3 encodes the sole SUN protein. Deletion of MPS3 or the conserved SUN domain is lethal in three different genetic backgrounds. Mutations in the SUN domain result in defects in duplication of the spindle pole body, the yeast centrosome-equivalent organelle. A genome-wide screen for mutants that exhibited synthetic fitness defects in combination with mps3 SUN domain mutants yielded a large number of hits in components of the spindle apparatus and the spindle checkpoint. Mutants in lipid metabolic processes and membrane organization also exacerbated the growth defects of mps3 SUN domain mutants, pointing to a role for Mps3 in nuclear membrane organization. Deletion of SLP1 or YER140W/EMP65 (for ER membrane protein of 65 kDa) aggravated growth of mps3 SUN domain mutants. Slp1 and Emp65 form an ER-membrane associated protein complex that is not required directly for spindle pole body duplication or spindle assembly. Rather, Slp1 is involved in Mps3 localization to the NE.
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