CoChat
Sign Up
Cited by 662

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

Deacetylation of Nuclear LC3 Drives Autophagy Initiation under Starvation

Huang, Rui, Xu, Yinfeng, Wan, Wei, Shou, Xin, Qian, Jiali, You, Zhiyuan, Liu, Bo, Chang, Chunmei, Zhou, Tianhua, Lippincott-Schwartz, Jennifer, Liu, Wei·2015·Molecular Cell
DOI 10.1016/j.molcel.2014.12.013
Open this paper in CoChat — free account

Abstract

Shuttling of macromolecules between different cellular compartments helps regulate the timing and extent of different cellular activities. Here, we report that LC3, a key initiator of autophagy that cycles between the nucleus and cytoplasm, becomes selectively activated in the nucleus during starvation through deacetylation by the nuclear deacetylase Sirt1. Deacetylation of LC3 at K49 and K51 by Sirt1 allows LC3 to interact with the nuclear protein DOR and return to the cytoplasm with DOR, where it is able to bind Atg7 and other autophagy factors and undergo phosphatidylethanolamine conjugation to preautophagic membranes. The association of deacetylated LC3 with autophagic factors shifts LC3's distribution from the nucleus toward the cytoplasm. Thus, an acetylation-deacetylation cycle ensures that LC3 effectively redistributes in an activated form from nucleus to cytoplasm, where it plays a central role in autophagy to enable the cell to cope with the lack of external nutrients.

Overview

Integrity signals

Registry

Crossref · 10.1016/j.molcel.2014.12.013

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 35

  1. Axe, 2008, Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum, J. Cell Biol., 182, 685, 10.1083/jcb.200803137 · DOI · Paper page
  2. Bernasconi, 2012, Role of the SEL1L:LC3-I complex as an ERAD tuning receptor in the mammalian ER, Mol. Cell, 46, 809, 10.1016/j.molcel.2012.04.017 · DOI
  3. Choudhary, 2009, Lysine acetylation targets protein complexes and co-regulates major cellular functions, Science, 325, 834, 10.1126/science.1175371 · DOI · Paper page
  4. Drake, 2010, Nucleocytoplasmic distribution and dynamics of the autophagosome marker EGFP-LC3, PLoS ONE, 5, e9806, 10.1371/journal.pone.0009806 · DOI
  5. Eskelinen, 2008, New insights into the mechanisms of macroautophagy in mammalian cells, Int Rev Cell Mol Biol, 266, 207, 10.1016/S1937-6448(07)66005-5 · DOI
  6. Füllgrabe, 2013, The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy, Nature, 500, 468, 10.1038/nature12313 · DOI
  7. Furuta, 2002, Light Chain 3 associates with a Sos1 guanine nucleotide exchange factor: its significance in the Sos1-mediated Rac1 signaling leading to membrane ruffling, Oncogene, 21, 7060, 10.1038/sj.onc.1205790 · DOI
  8. Gao, 2010, Processing of autophagic protein LC3 by the 20S proteasome, Autophagy, 6, 126, 10.4161/auto.6.1.10928 · DOI
  9. Guo, 2012, AP1 is essential for generation of autophagosomes from the trans-Golgi network, J. Cell Sci., 125, 1706, 10.1242/jcs.093203 · DOI
  10. Hailey, 2010, Mitochondria supply membranes for autophagosome biogenesis during starvation, Cell, 141, 656, 10.1016/j.cell.2010.04.009 · DOI
  11. Hong, 2011, Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8, Nat. Struct. Mol. Biol., 18, 1323, 10.1038/nsmb.2165 · DOI
  12. Ichimura, 2000, A ubiquitin-like system mediates protein lipidation, Nature, 408, 488, 10.1038/35044114 · DOI
  13. Jin, 2007, Cytoplasm-localized SIRT1 enhances apoptosis, J. Cell. Physiol., 213, 88, 10.1002/jcp.21091 · DOI
  14. Kamada, 2000, Tor-mediated induction of autophagy via an Apg1 protein kinase complex, J. Cell Biol., 150, 1507, 10.1083/jcb.150.6.1507 · DOI · Paper page
  15. Klionsky, 2007, Autophagy: from phenomenology to molecular understanding in less than a decade, Nat. Rev. Mol. Cell Biol., 8, 931, 10.1038/nrm2245 · DOI
  16. Kraft, 2014, Size, stoichiometry, and organization of soluble LC3-associated complexes, Autophagy, 10, 861, 10.4161/auto.28175 · DOI
  17. Lee, 2009, Regulation of autophagy by the p300 acetyltransferase, J. Biol. Chem., 284, 6322, 10.1074/jbc.M807135200 · DOI · Paper page
  18. Lee, 2008, A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy, Proc. Natl. Acad. Sci. USA, 105, 3374, 10.1073/pnas.0712145105 · DOI
  19. Lin, 2012, GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to autophagy, Science, 336, 477, 10.1126/science.1217032 · DOI · Paper page
  20. Mauvezin, 2010, The nuclear cofactor DOR regulates autophagy in mammalian and Drosophila cells, EMBO Rep., 11, 37, 10.1038/embor.2009.242 · DOI
  21. Michishita, 2005, Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins, Mol. Biol. Cell, 16, 4623, 10.1091/mbc.E05-01-0033 · DOI · Paper page
  22. Mizushima, 2007, Autophagy: process and function, Genes Dev., 21, 2861, 10.1101/gad.1599207 · DOI
  23. Mizushima, 2010, Methods in mammalian autophagy research, Cell, 140, 313, 10.1016/j.cell.2010.01.028 · DOI · Paper page
  24. Nakatogawa, 2007, Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion, Cell, 130, 165, 10.1016/j.cell.2007.05.021 · DOI
  25. Noda, 2010, Atg8-family interacting motif crucial for selective autophagy, FEBS Lett., 584, 1379, 10.1016/j.febslet.2010.01.018 · DOI
  26. Noda, 2011, Structural basis of Atg8 activation by a homodimeric E1, Atg7, Mol. Cell, 44, 462, 10.1016/j.molcel.2011.08.035 · DOI
  27. Nowak, 2009, The TP53INP2 protein is required for autophagy in mammalian cells, Mol. Biol. Cell, 20, 870, 10.1091/mbc.E08-07-0671 · DOI
  28. Pankiv, 2010, FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport, J. Cell Biol., 188, 253, 10.1083/jcb.200907015 · DOI
  29. Reggiori, 2010, Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication, Cell Host Microbe, 7, 500, 10.1016/j.chom.2010.05.013 · DOI
  30. Tang, 2010, Endogenous HMGB1 regulates autophagy, J. Cell Biol., 190, 881, 10.1083/jcb.200911078 · DOI · Paper page
  31. Waters, 2009, Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover, FEBS Lett., 583, 1846, 10.1016/j.febslet.2009.04.049 · DOI
  32. Wei, 2013, EGFR-mediated Beclin 1 phosphorylation in autophagy suppression, tumor progression, and tumor chemoresistance, Cell, 154, 1269, 10.1016/j.cell.2013.08.015 · DOI · Paper page
  33. Yi, 2012, Function and molecular mechanism of acetylation in autophagy regulation, Science, 336, 474, 10.1126/science.1216990 · DOI
  34. Zhou, 1998, Microtubule involvement in translational regulation of fibronectin expression by light chain 3 of microtubule-associated protein 1 in vascular smooth muscle cells, Circ. Res., 83, 481, 10.1161/01.RES.83.5.481 · DOI
  35. Zhou, 1997, Microtubule-associated protein 1 light chain 3 is a fibronectin mRNA-binding protein linked to mRNA translation in lamb vascular smooth muscle cells, J. Clin. Invest., 100, 3070, 10.1172/JCI119862 · DOI

Cited by

Sorted by citations

Metadata

Authors
Huang, R., Xu, Y., Wan, W., Shou, X., Qian, J., You, Z., Liu, B., Chang, C., Zhou, T., Lippincott-Schwartz, J., & Liu, W.
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2015-02
Volume
57
Issue
3
Pages
456-466
ISSN
1097-2765
DOI
10.1016/j.molcel.2014.12.013
Cited by
662
References
6
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review