ArticleNature communications2018
Steric exclusion and protein conformation determine the localization of plasma membrane transporters.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 77 citations in OpenAlex.
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- Microdomain Protein Nce102 Is a Local Sensor of Plasma Membrane Sphingolipid Balance.Microbiology spectrum · 2022Article
- Membrane thickness, lipid phase and sterol type are determining factors in the permeability of membranes to small solutes.Nature communications · 2022Article
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- The Rpd3-Complex Regulates Expression of Multiple Cell Surface Recycling Factors in Yeast.International journal of molecular sciences · 2021Article
- Structure and activation mechanism of the hexameric plasma membrane HNature communications · 2021Article
- The Sur7 cytoplasmic C terminus regulates morphogenesis and stress responses in Candida albicans.Molecular microbiology · 2021Article
- The Bul1/2 Alpha-Arrestins Promote Ubiquitylation and Endocytosis of the Can1 Permease upon Cycloheximide-Induced TORC1-Hyperactivation.International journal of molecular sciences · 2021Article
- Cryo-Electron Tomography of Candida glabrata Plasma Membrane Proteins.Journal of fungi (Basel, Switzerland) · 2021Article
- A glucose-starvation response governs endocytic trafficking and eisosomal retention of surface cargoes in budding yeast.Journal of cell science · 2021Article
- Cellular dynamics of the SecA ATPase at the single molecule level.Scientific reports · 2021Article
- Endocytosis of nutrient transporters in fungi: The ART of connecting signaling and trafficking.Computational and structural biotechnology journal · 2021Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
The plasma membrane (PM) of Saccharomyces cerevisiae contains membrane compartments, MCC/eisosomes and MCPs, named after the protein residents Can1 and Pma1, respectively. Using high-resolution fluorescence microscopy techniques we show that Can1 and the homologous transporter Lyp1 are able to diffuse into the MCC/eisosomes, where a limited number of proteins are conditionally trapped at the (outer) edge of the compartment. Upon addition of substrate, the immobilized proteins diffuse away from the MCC/eisosomes, presumably after taking a different conformation in the substrate-bound state. Our data indicate that the mobile fraction of all integral plasma membrane proteins tested shows extremely slow Brownian diffusion through most of the PM. We also show that proteins with large cytoplasmic domains, such as Pma1 and synthetic chimera of Can1 and Lyp1, are excluded from the MCC/eisosomes. We hypothesize that the distinct localization patterns found for these integral membrane proteins in S. cerevisiae arises from a combination of slow lateral diffusion, steric exclusion, and conditional trapping in membrane compartments.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.