Evidence map›Paper›PMID 26728248›Full record

ArticleTraffic (Copenhagen, Denmark)2016

Nuclear LC3 Associates with Slowly Diffusing Complexes that Survey the Nucleolus.

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

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
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  3. Review
  4. Article
  5. Article
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  11. Article
  12. Review
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  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Emerging Role of the Nucleolar Stress Response in Autophagy.Frontiers in cellular neuroscience · 2019
    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

4 authors.

Lewis J KraftChemical and Physical Biology Program, Vanderbilt University, Nashville, TN, USA.
Pallavi ManralDepartment of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN, USA.
Jacob DowlerDepartment of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN, USA.
Anne K KenworthyChemical and Physical Biology Program, Vanderbilt University, Nashville, TN, USA.

Funding

The Vanderbilt Institute for Clinical and Translational Research (VICTR)UL1TR000445 · NCATS · VANDERBILT UNIVERSITY MEDICAL CENTER · PI BERNARD, GORDON RAPHAEL · 2012 to 2016
$41.4M
Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI OWEN P MCGUINNESS · 2012 to 2026
$29.3M
TRANSGENIC MOUSE/ ES CELL SHARES RESOURCESP60DK020593 · NIDDK · VANDERBILT UNIVERSITY · PI MCGUINNESS, OWEN P · 1986 to 2011
$28.1M
NCATS NIH HHS UL1 TR000445NCATS NIH HHS UL1TR000445NIDDK NIH HHS DK020593NIDDK NIH HHS P30 DK020593
6 · The paper itself

Abstract

MAP1LC3B (microtubule-associated protein 1 light chain 3, LC3) is a key component of the autophagy pathway, contributing to both cargo selection and autophagosome formation in the cytoplasm. Emerging evidence suggests that nuclear forms of LC3 are also functionally important; however, the mechanisms that facilitate the nuclear targeting and trafficking of LC3 between the nucleus and cytoplasm under steady-state conditions are poorly understood. In this study, we examine how residues known to regulate the interactions between LC3 and other proteins or RNA (F52 L53, R68-R70 and G120) contribute to its nuclear targeting, nucleocytoplasmic transport and association with nucleoli and other nuclear components. We find that residues F52 L53 and R68-70, but not G120, regulate targeting of LC3 to the nucleus, its rates of nucleocytoplasmic transport and the apparent sizes of LC3-associated complexes in the nucleus inferred from fluorescence recovery after photobleaching (FRAP) measurements. We also show that LC3 is enriched in nucleoli and its triple arginine motif is especially important for nucleolar targeting. Finally, we identify a series of candidate nuclear LC3-interacting proteins using mass spectrometry, including MAP1B, tubulin and several 40S ribosomal proteins. These findings suggest LC3 is retained in the nucleus in association with high-molecular weight complexes that continuously scan the nucleolus.

Indexed as

Active Transport, Cell NucleusCell NucleolusHeLa CellsHumansMicrotubule-Associated ProteinsProtein BindingRibosomal ProteinsRNATubulinMAP1LC3B protein, humanMicrotubule-Associated ProteinsRibosomal ProteinsRNATubulinautophagydiffusionFRAPMAP1LC3mass spectrometryMudPITnucleo-cytoplasmic transportnucleus

Identifiers

PMID26728248
PMCPMC4975375

What OpenQuestion holds

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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.