ArticleBiophysical journal2014
Tracking single serotonin transporter molecules at the endoplasmic reticulum and plasma membrane.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Role of Serotonin on Gene Expression and Physiology in Human Cytotrophoblasts and Placenta.Endocrinology · 2025Article
- Article
- Cooperative Binding of Substrate and Ions Drives Forward Cycling of the Human Creatine Transporter-1.Frontiers in physiology · 2022Article
- Functional and Biochemical Consequences of Disease Variants in Neurotransmitter Transporters: A Special Emphasis on Folding and Trafficking Deficits.Pharmacology & therapeutics · 2021Review
- SLC6 transporter oligomerization.Journal of neurochemistry · 2021Review
- A Novel Biotinylated Homotryptamine Derivative for Quantum Dot Imaging of Serotonin Transporter in Live Cells.Frontiers in cellular neuroscience · 2021Article
- How to rescue misfolded SERT, DAT and NET: targeting conformational intermediates with atypical inhibitors and partial releasers.Biochemical Society transactions · 2019Review
- Dopamine transporter oligomerization involves the scaffold domain, but spares the bundle domain.PLoS computational biology · 2018Article
- Functional properties of dopamine transporter oligomers after copper linking.Journal of neurochemistry · 2018Article
- Pharmacochaperoning in aThe Journal of biological chemistry · 2017Article
- Single-molecule fluorescence microscopy review: shedding new light on old problems.Bioscience reports · 2017Review
- Direct PIPNature communications · 2017Article
- When transporters fail to be transported: how to rescue folding-deficient SLC6 transporters.Journal of neurology & neuromedicine · 2016Article
- Dopamine transporter oligomerization: impact of combining protomers with differential cocaine analog binding affinities.Journal of neurochemistry · 2015Article
- Amphetamines, new psychoactive drugs and the monoamine transporter cycle.Trends in pharmacological sciences · 2015Review
- Single-molecule analysis of diffusion and trapping of STIM1 and Orai1 at endoplasmic reticulum-plasma membrane junctions.Molecular biology of the cell · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transmembrane proteins are synthesized and folded in the endoplasmic reticulum (ER), an interconnected network of flattened sacs or tubes. Up to now, this organelle has eluded a detailed analysis of the dynamics of its constituents, mainly due to the complex three-dimensional morphology within the cellular cytosol, which precluded high-resolution, single-molecule microscopy approaches. Recent evidences, however, pointed out that there are multiple interaction sites between ER and the plasma membrane, rendering total internal reflection microscopy of plasma membrane proximal ER regions feasible. Here we used single-molecule fluorescence microscopy to study the diffusion of the human serotonin transporter at the ER and the plasma membrane. We exploited the single-molecule trajectories to map out the structure of the ER close to the plasma membrane at subdiffractive resolution. Furthermore, our study provides a comparative picture of the diffusional behavior in both environments. Under unperturbed conditions, the majority of proteins showed similar mobility in the two compartments; at the ER, however, we found an additional 15% fraction of molecules moving with 25-fold faster mobility. Upon degradation of the actin skeleton, the diffusional behavior in the plasma membrane was strongly influenced, whereas it remained unchanged in the ER.
Indexed as
Identifiers
What OpenQuestion holds
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.