ArticleThe Journal of cell biology2008
Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum.
Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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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
50 citing papers in PubMed.
- Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Viruses · 2026Article
- Mechanisms of COPII coat assembly and cargo recognition in the secretory pathway.Nature reviews. Molecular cell biology · 2025Review
- Article
- C-terminal tagging, transmembrane domain hydrophobicity, and an ER retention motif influence the secretory trafficking of the inner nuclear membrane protein emerin.bioRxiv : the preprint server for biology · 2025Article
- The Dsc ubiquitin ligase complex identifies transmembrane degrons to degrade orphaned proteins at the Golgi.Nature communications · 2024Article
- Partitioning into ER membrane microdomains impacts autophagic protein turnover during cellular aging.Scientific reports · 2024Article
- FT-GPI, a highly sensitive and accurate predictor of GPI-anchored proteins, reveals the composition and evolution of the GPI proteome in Plasmodium species.Malaria journal · 2023Article
- Review
- The WRB Subunit of the Get3 Receptor is Required for the Correct Integration of its Partner CAML into the ER.Scientific reports · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Protein Partitioning into Ordered Membrane Domains: Insights from Simulations.Biophysical journal · 2018Article
- Lateral diffusion and signaling of receptor for advanced glycation end-products (RAGE): a receptor involved in chronic inflammation.European biophysics journal : EBJ · 2018Article
- SOD1 stimulates lamellipodial protrusions in Neuro 2A cell lines.Communicative & integrative biology · 2018Article
- Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion.Annual review of cell and developmental biology · 2017Review
- Maize opaque10 Encodes a Cereal-Specific Protein That Is Essential for the Proper Distribution of Zeins in Endosperm Protein Bodies.PLoS genetics · 2016Article
- De novo peroxisome biogenesis: Evolving concepts and conundrums.Biochimica et biophysica acta · 2016Review
- SSH Analysis of Endosperm Transcripts and Characterization of Heat Stress Regulated Expressed Sequence Tags in Bread Wheat.Frontiers in plant science · 2016Article
- TM9 family proteins control surface targeting of glycine-rich transmembrane domains.Journal of cell science · 2015Article
- Trafficking of plant plasma membrane aquaporins: multiple regulation levels and complex sorting signals.Plant & cell physiology · 2015Review
- Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease.Scientific reports · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The length and hydrophobicity of the transmembrane domain (TMD) play an important role in the sorting of membrane proteins within the secretory pathway; however, the relative contributions of protein-protein and protein-lipid interactions to this phenomenon are currently not understood. To investigate the mechanism of TMD-dependent sorting, we used the following two C tail-anchored fluorescent proteins (FPs), which differ only in TMD length: FP-17, which is anchored to the endoplasmic reticulum (ER) membrane by 17 uncharged residues, and FP-22, which is driven to the plasma membrane by its 22-residue-long TMD. Before export of FP-22, the two constructs, although freely diffusible, were seen to distribute differently between ER tubules and sheets. Analyses in temperature-blocked cells revealed that FP-17 is excluded from ER exit sites, whereas FP-22 is recruited to them, although it remains freely exchangeable with the surrounding reticulum. Thus, physicochemical features of the TMD influence sorting of membrane proteins both within the ER and at the ER-Golgi boundary by simple receptor-independent mechanisms based on partitioning.
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Registered trials
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.