Evidence map›Paper›PMID 26686281›Full record

ReviewBiochimica et biophysica acta2016

SMP-domain proteins at membrane contact sites: Structure and function.

Karin M Reinisch, Pietro De Camilli

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. LYVAC/PDZD8 is a lysosomal vacuolator.Science (New York, N.Y.) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023
    Review
  10. Article
  11. Review
  12. Lipid Transport from Endoplasmic Reticulum to Autophagic Membranes.Cold Spring Harbor perspectives in biology · 2022
    Review
  13. Article
  14. Article
  15. Quantitative Models of Lipid Transfer and Membrane Contact Formation.Contact (Thousand Oaks (Ventura County, Calif.)) · 2022
    Article
  16. Article
  17. Article
  18. Emerging perspectives on multidomain phosphatidylinositol transfer proteins.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  19. Article
  20. Review
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

2 authors at 2 institutions in 1 country.

Karin M ReinischDepartment of Cell Biology, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA. Electronic address: karin.reinisch@yale.edu.
Pietro De CamilliDepartment of Cell Biology, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA; Department of Neurobiology, Howard Hughes Medical Institute, Kavli Institute for Neuroscience and Program in Cellular Neuroscience, Neurodegeneration, and Repair, Yale University School of Medicine, New Haven, CT 06510, USA. Electronic address: pietro.decamilli@yale.edu.
Howard Hughes Medical Institute · USYale University · US

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Yale/NIDA Neuroproteomics Research CenterP30DA018343 · NIDA · YALE UNIVERSITY · PI Marina R Picciotto · 2004 to 2026
$37.1M
Regulatory Mechanisms in Membrane TraffickingR01GM080616 · NIGMS · YALE UNIVERSITY · PI REINISCH, KARIN M · 2007 to 2018
$4.1M
Molecular Mechanisms in Synaptic Vesicle RecyclingR37NS036251 · NINDS · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 2010 to 2016
$2.7M
OCRL and the pathogenesis of Lowe Syndrome and Dent DiseaseR01DK082700 · NIDDK · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 2009 to 2016
$2.4M
Pathophysiology of Plasma Membrane PI4P GenerationR01GM114068 · NIGMS · YALE UNIVERSITY · PI REINISCH, KARIN M · 2015 to 2018
$2.0M
Howard Hughes Medical InstituteNCATS NIH HHS UL1 TR001863NIDA NIH HHS P30 DA018343NIDDK NIH HHS DK082700NIDDK NIH HHS R01 DK082700NIGMS NIH HHS GM080616NIGMS NIH HHS GM114068NIGMS NIH HHS R01 GM080616NIGMS NIH HHS R01 GM114068NINDS NIH HHS R37 NS036251NINDS NIH HHS R37NS036251
6 · The paper itself

Abstract

SMP-domains are found in proteins that localize to membrane contact sites. Elucidation of the properties of these proteins gives clues as to the molecular bases underlying processes that occur at such sites. Described here are recent discoveries concerning the structure, function, and regulation of the Extended-Synaptotagmin proteins and ERMES complex subunits, SMP-domain proteins at endoplasmic reticulum (ER)-plasma membrane and ER-mitochondrial contacts, respectively. They act as tethers contributing to the architecture of these sites and as lipid transporters that convey glycerolipids between apposed membranes. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.

Indexed as

AnimalsCell MembraneEndoplasmic ReticulumHumansMembrane ProteinsMitochondriaMitochondrial MembranesProtein Structure, TertiaryStructure-Activity RelationshipSynaptotagminsMembrane ProteinsSynaptotagmins

Identifiers

PMID26686281
PMCPMC4902782
OpenAlexW2198206486

What OpenQuestion holds

Textmetadata
LicenceTDM
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.