Evidence map›Paper›PMID 27442348›Full record

ArticleAutophagy2016

Size, organization, and dynamics of soluble SQSTM1 and LC3-SQSTM1 complexes in living cells.

Lewis J Kraft, Jacob Dowler, Pallavi Manral, Anne K Kenworthy

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. SQSTM1eNeurologicalSci · 2021
    Article
  8. Article
  9. Article
  10. A current view of molecular dissection in autophagy machinery.Journal of physiology and biochemistry · 2020
    Review
  11. Article
  12. Article
  13. Article
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

4 authors at 1 institution in 1 country.

Lewis J Krafta Chemical and Physical Biology Program , Vanderbilt University Medical Center , Nashville , TN , USA.
Jacob Dowlerb Department of Molecular Physiology and Biophysics , Vanderbilt University Medical Center , Nashville , TN , USA.
Pallavi Manralb Department of Molecular Physiology and Biophysics , Vanderbilt University Medical Center , Nashville , TN , USA.
Anne K Kenworthya Chemical and Physical Biology Program , Vanderbilt University Medical Center , Nashville , TN , USA.
Vanderbilt University Medical Center · US

Funding

Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI OWEN P MCGUINNESS · 2012 to 2026
$29.3M
NIDDK NIH HHS P30 DK020593
6 · The paper itself

Abstract

Selective macroautophagy/autophagy-with the help of molecular receptors-captures cargo for lysosomal degradation. Among the best-studied molecular receptors is SQSTM1/p62, a homo-oligomeric ubiquitin binding protein, which binds to both cargo and MAP1LC3B/LC3, a protein important for autophagosome biogenesis. Although the mechanisms underlying interaction of LC3 and SQSTM1 have been extensively studied, very little is known about the size or organization of soluble complexes formed between SQSTM1 and LC3 prior to phagophore (the autophagosome precursor) binding in live cells at the molecular level. To address this question, in the current study we use a combination of 2 microscopy-based approaches, FRET microscopy and confocal FRAP, to study the nanoscale properties of soluble SQSTM1 complexes and SQSTM1-LC3 complexes in living HeLa cells. We find that, independent of puncta, SQSTM1 oligomerizes to form very slowly diffusing complexes that contain multiple copies of SQSTM1 within FRET proximity of one another. Furthermore, we show that the interactions of soluble pools of LC3 and SQSTM1 can be readily detected by both FRAP and FRET. Finally, we uncover unexpected roles of SQSTM1's PB1 domain, a region of the protein involved in homo-oligomer formation, in complex formation. Taken together, these findings provide new insights into the nature of nanometer-sized protein complexes in the autophagy pathway.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsAutophagyAutophagy-Related Protein 8 FamilyCell NucleusCytoplasmCytosolFluorescence Resonance Energy TransferHeLa CellsHumansLysosomesMiceMicroscopy, ConfocalMicrotubule-Associated ProteinsPhagosomesProtein BindingAdaptor Proteins, Signal TransducingAutophagy-Related Protein 8 FamilyGABARAPL2 protein, humanMAP1LC3A protein, humanMap1lc3b protein, mouseMicrotubule-Associated ProteinsSequestosome-1 ProteinSQSTM1 protein, humanSqstm1 protein, mouseUbiquitinATG8autophagydiffusionfluorescenceFRAPFREThydrodynamic radiusMAP1LC3SQSTM1

Identifiers

PMID27442348
PMCPMC5082789
OpenAlexW2503448060

What OpenQuestion holds

Textmetadata
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.