ReviewFrontiers in plant science2013
Homotypic fusion of endoplasmic reticulum membranes in plant cells.
Review in Frontiers in plant science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed.
- Connecting tubules: mechanisms of endoplasmic reticulum membrane fusion.Biochemical Society transactions · 2025Review
- Review
- Human atlastins are sufficient to drive the fusion of liposomes with a physiological lipid composition.The Journal of cell biology · 2023Article
- Quantitative analysis of plant ER architecture and dynamics.Nature communications · 2019Article
- Atlastin-1 regulates morphology and function of endoplasmic reticulum in dendrites.Nature communications · 2019Article
- Atlastin regulates store-operated calcium entry for nerve growth factor-induced neurite outgrowth.Scientific reports · 2017Article
- SNAREs support atlastin-mediated homotypic ER fusion in Saccharomyces cerevisiae.The Journal of cell biology · 2015Article
- Putting the Squeeze on Plasmodesmata: A Role for Reticulons in Primary Plasmodesmata Formation.Plant physiology · 2015Article
- Human atlastin GTPases mediate differentiated fusion of endoplasmic reticulum membranes.Protein & cell · 2015Article
- ER network dynamics are differentially controlled by myosins XI-K, XI-C, XI-E, XI-I, XI-1, and XI-2.Frontiers in plant science · 2014Article
- Specialized membrane domains of plasmodesmata, plant intercellular nanopores.Frontiers in plant science · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
The endoplasmic reticulum (ER) is a membrane-bounded organelle whose membrane comprises a network of tubules and sheets. The formation of these characteristic shapes and maintenance of their continuity through homotypic membrane fusion appears to be critical for the proper functioning of the ER. The atlastins (ATLs), a family of ER-localized dynamin-like GTPases, have been identified as fusogens of the ER membranes in metazoans. Mutations of the ATL proteins in mammalian cells cause morphological defects in the ER, and purified Drosophila ATL mediates membrane fusion in vitro. Plant cells do not possess ATL, but a family of similar GTPases, named root hair defective 3 (RHD3), are likely the functional orthologs of ATLs. In this review, we summarize recent advances in our understanding of how RHD3 proteins play a role in homotypic ER fusion. We also discuss the possible physiological significance of forming a tubular ER network in plant cells.
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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.