Evidence map›Paper›PMID 14581454›Full record

ArticleThe Journal of cell biology2003

Formation of stacked ER cisternae by low affinity protein interactions.

Erik L Snapp, Ramanujan S Hegde, Maura Francolini, Francesca Lombardo, Sara Colombo, Emanuela Pedrazzini, Nica Borgese, Jennifer Lippincott-Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers.

0numbers the graph read from it
0cells of the map it votes in
248citing papers in PubMed
7.2field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

248 citing papers in PubMed, 470 citations in OpenAlex.

  1. Review
  2. Honeydew: A Fluorescent Aptamer for Low-Cost Azo Food Dyes.Chembiochem : a European journal of chemical biology · 2026
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  16. Protein interactions, calcium, phosphorylation, and cholesterol modulate CFTR cluster formation on membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
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  20. Article

188 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Erik L SnappCell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, 18 Library Dr., Bldg. 18T, Rm. 101, Bethesda, MD 20892, USA. jlippin@helix.nih.gov
Ramanujan S Hegde
Maura Francolini
Francesca Lombardo
Sara Colombo
Emanuela Pedrazzini
Nica Borgese
Jennifer Lippincott-Schwartz
National Institutes of Health · USIstituto di Biologia e Biotecnologia Agraria · ITMagna Graecia University · ITUniversity of Milan · IT

Funding

Organization and Dynamics of Endomembrane Pathways and OrganellesZIAHD001609 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2019
$16.2M
Secretory Membrane Trafficking/Sorting/CompartmentalizatZ01HD001609 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI LIPPINCOTT-SCHWARTZ, JENNIFER · 1992 to 2008
$3.1M
Regulation of Protein Translocation into the ERZ01HD008752 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI HEGDE, RAMANUJAN S · 2002 to 2008
$1.0M
Regulation of Protein Translocation into the ERZIAHD008752 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI HEGDE, RAMANUJAN S · 2009 to 2011
$561k
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) can transform from a network of branching tubules into stacked membrane arrays (termed organized smooth ER [OSER]) in response to elevated levels of specific resident proteins, such as cytochrome b(5). Here, we have tagged OSER-inducing proteins with green fluorescent protein (GFP) to study OSER biogenesis and dynamics in living cells. Overexpression of these proteins induced formation of karmellae, whorls, and crystalloid OSER structures. Photobleaching experiments revealed that OSER-inducing proteins were highly mobile within OSER structures and could exchange between OSER structures and surrounding reticular ER. This indicated that binding interactions between proteins on apposing stacked membranes of OSER structures were not of high affinity. Addition of GFP, which undergoes low affinity, antiparallel dimerization, to the cytoplasmic domains of non-OSER-inducing resident ER proteins was sufficient to induce OSER structures when overexpressed, but addition of a nondimerizing GFP variant was not. These results point to a molecular mechanism for OSER biogenesis that involves weak homotypic interactions between cytoplasmic domains of proteins. This mechanism may underlie the formation of other stacked membrane structures within cells.

Indexed as

AnimalsCell LineChlorocebus aethiopsCOS CellsEndoplasmic ReticulumEndoplasmic Reticulum, SmoothGreen Fluorescent ProteinsIntracellular MembranesLuminescent ProteinsMembrane ProteinsModels, BiologicalPoint MutationProtein Structure, TertiaryRecombinant Fusion ProteinsGreen Fluorescent ProteinsLuminescent ProteinsMembrane ProteinsRecombinant Fusion Proteins

Identifiers

PMID14581454
PMCPMC2173526
OpenAlexW2153291568

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.