ArticleTraffic (Copenhagen, Denmark)2012
The formation and stability of DC-SIGN microdomains require its extracellular moiety.
Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 23 citations in OpenAlex.
- Multiscale imaging and quantitative analysis of plasma membrane protein-cortical actin interplay.Biophysical journal · 2023Article
- Multiscale imaging and quantitative analysis of plasma membrane protein-cortical actin interplay.bioRxiv : the preprint server for biology · 2023Article
- Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation.International journal of environmental research and public health · 2022Review
- Dectin-1-Mediated DC-SIGN Recruitment toLife (Basel, Switzerland) · 2021Article
- Fluorescence strategies for mapping cell membrane dynamics and structures.APL bioengineering · 2020Article
- Toward a new picture of the living plasma membrane.Protein science : a publication of the Protein Society · 2020Review
- Review
- Fine Mapping the Interaction Between Dendritic Cell-Specific Intercellular Adhesion Molecule (ICAM)-3-Grabbing Nonintegrin and the Cytomegalovirus Envelope Glycoprotein B.The Journal of infectious diseases · 2018Article
- Beyond attachment: Roles of DC-SIGN in dengue virus infection.Traffic (Copenhagen, Denmark) · 2017Article
- Dynamics of the actin cytoskeleton mediates receptor cross talk: An emerging concept in tuning receptor signaling.The Journal of cell biology · 2016Review
- Nanoclustering as a dominant feature of plasma membrane organization.Journal of cell science · 2014Review
- Super-resolution imaging of C-type lectin spatial rearrangement within the dendritic cell plasma membrane at fungal microbe contact sites.Frontiers in physics · 2014Article
- Low copy numbers of DC-SIGN in cell membrane microdomains: implications for structure and function.Traffic (Copenhagen, Denmark) · 2014Article
- The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells.The Journal of biological chemistry · 2012Article
- Super-resolution imaging of C-type lectin and influenza hemagglutinin nanodomains on plasma membranes using blink microscopy.Biophysical journal · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Dendritic cell-specific intercellular adhesion molecule (ICAM)-3-grabbing non-integrin (DC-SIGN) is a Ca(2+) -dependent transmembrane lectin that binds a large variety of pathogens and facilitates their uptake for subsequent antigen presentation. This receptor is present in cell surface microdomains, but factors involved in microdomain formation and their exceptional stability are not clear. To determine which domain/motif of DC-SIGN facilitates its presence in microdomains, we studied mutations at key locations including truncation of the cytoplasmic tail, and ectodomain mutations that resulted in the removal of the N-linked glycosylation site, the tandem repeats and the carbohydrate recognition domain (CRD), as well as modification of the calcium sites in the CRD required for carbohydrate binding. Confocal imaging and fluorescence recovery after photobleaching measurements showed that the cytoplasmic domain and the N-linked glycosylation site do not affect the ability of DC-SIGN to form stable microdomains. However, truncation of the CRD results in complete loss of visible microdomains and subsequent lateral diffusion of the mutants. Apart from cell adhesions, membrane domains are thought to be localized primarily via the cytoskeleton. By contrast, we propose that interactions between the CRD of DC-SIGN and the extracellular matrix and/or cis interactions with transmembrane scaffolding protein(s) play an essential role in organizing these microdomains.
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.