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TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis
Open accessAbstract
SUMMARY Selective autophagy performs an array of tasks to maintain intracellular homeostasis, sterility, and organellar and cellular functionality. The fidelity of these processes depends on precise target recognition and limited activation of the autophagy apparatus in a localized fashion. Here we describe cooperation in such processes between the TRIM family and Galectin family of proteins. TRIMs, which are E3 ubiquitin ligases, displayed propensity to associate with Galectins. One specific TRIM, TRIM16, interacted with Galectin-3 in an ULK1-dependent manner. TRIM16, through integration of Galectin- and ubiquitin-based processes, coordinated recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1, ULK1, and Beclin 1 in response to damaged endomembranes. TRIM16 affected mTOR, interacted with TFEB and influenced TFEB’s nuclear translocation. The cooperation between TRIM16 and Galectin-3 in targeting and activation of selective autophagy protects cells from lysosomal damage and Mycobacterium tuberculosis invasion.
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Citations
Cites
Genome engineering using the CRISPR-Cas9 system
Ran, F. A., Hsu, P. D., Wright, J., Agarwala, V., Scott, D. A., & Zhang, F. (2013) · Nature Protocols · doi:10.1038/nprot.2013.143 · Cited by 11,133
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
The Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978
Autophagy in infection, inflammation and immunity
Deretic, V., Saitoh, T., & Akira, S. (2013) · Nature Reviews Immunology · doi:10.1038/nri3532 · Cited by 1,919
Self-citationPeterson, T. R., Laplante, M., Thoreen, C. C., Sancak, Y., Kang, S. A., Kuehl, W. M., Gray, N. S., & Sabatini, D. M. (2009) · Cell · doi:10.1016/j.cell.2009.03.046 · Cited by 1,202
Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
Thurston, T. L. M., Wandel, M. P., von Muhlinen, N., Foeglein, Á., & Randow, F. (2012) · Nature · doi:10.1038/nature10744 · Cited by 1,034
Regulation of mTORC1 by amino acids
Bar-Peled, L., & Sabatini, D. M. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.03.003 · Cited by 773
Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury
Maejima, I., Takahashi, A., Omori, H., Kimura, T., Takabatake, Y., Saitoh, T., Yamamoto, A., Hamasaki, M., Noda, T., Isaka, Y., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.171 · Cited by 642 · cited 26×
“Galectins participate in autophagic response to endomembrane perforations caused by lysosomal damaging agents and by bacteria (Fujita et al., 2013; Maejima et al., 2013; Thurston et al., 2012).”
BackgroundMethodResultInfluentialSelf-citation
Cited by
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Self-citationBiological Functions of Autophagy Genes: A Disease Perspective
Levine, B., & Kroemer, G. (2019) · Cell · doi:10.1016/j.cell.2018.09.048 · Cited by 2,832
Molecular definitions of autophagy and related processes
Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646
Self-citationLysosomes as dynamic regulators of cell and organismal homeostasis
Ballabio, A., & Bonifacino, J. S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0185-4 · Cited by 1,469
The mechanisms and roles of selective autophagy in mammals
Vargas, J. N. S., Hamasaki, M., Kawabata, T., Youle, R. J., & Yoshimori, T. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00542-2 · Cited by 1,016
Autophagy in inflammation, infection, and immunometabolism
Deretic, V. (2021) · Immunity · doi:10.1016/j.immuni.2021.01.018 · Cited by 862
Self-citationYim, W. W.-Y., & Mizushima, N. (2020) · Cell Discovery · doi:10.1038/s41421-020-0141-7 · Cited by 803
Autophagy balances inflammation in innate immunity
Deretic, V., & Levine, B. (2018) · Autophagy · doi:10.1080/15548627.2017.1402992 · Cited by 563
Self-citationTriggered recruitment of ESCRT machinery promotes endolysosomal repair
Skowyra, M. L., Schlesinger, P. H., Naismith, T. V., & Hanson, P. I. (2018) · Science · doi:10.1126/science.aar5078 · Cited by 578
The role of ubiquitination and deubiquitination in cancer metabolism
Sun, T., Liu, Z., & Yang, Q. (2020) · Molecular Cancer · doi:10.1186/s12943-020-01262-x · Cited by 508
Selective autophagy of intracellular organelles: Recent research advances
Li, W., He, P., Huang, Y., Li, Y.-F., Lu, J., Li, M., Kurihara, H., Luo, Z., Meng, T., Onishi, M., et al. (2021) · Theranostics · doi:10.7150/thno.49860 · Cited by 507
Galectin-3 Coordinates a Cellular System for Lysosomal Repair and Removal
Jia, J., Claude-Taupin, A., Gu, Y., Choi, S. W., Peters, R., Bissa, B., Mudd, M. H., Allers, L., Pallikkuth, S., Lidke, K. A., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2019.10.025 · Cited by 434
Self-citationYao, R.-Q., Ren, C., Xia, Z.-F., & Yao, Y.-M. (2021) · Autophagy · doi:10.1080/15548627.2020.1725377 · Cited by 441
Rusmini, P., Cortese, K., Crippa, V., Cristofani, R., Cicardi, M. E., Ferrari, V., Vezzoli, G., Tedesco, B., Meroni, M., Messi, E., et al. (2019) · Autophagy · doi:10.1080/15548627.2018.1535292 · Cited by 436
Mechanisms of Selective Autophagy
Lamark, T., & Johansen, T. (2021) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120219-035530 · Cited by 429
Self-citationDiverse Cellular Roles of Autophagy
Morishita, H., & Mizushima, N. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125300 · Cited by 376
Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins
Flavin, W. P., Bousset, L., Green, Z. C., Chu, Y., Skarpathiotis, S., Chaney, M. J., Kordower, J. H., Melki, R., & Campbell, E. M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1722-x · Cited by 258
Autophagy and organelle homeostasis in cancer
Miller, D. R., & Thorburn, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.010 · Cited by 258
Mehto, S., Jena, K. K., Nath, P., Chauhan, S., Kolapalli, S. P., Das, S. K., Sahoo, P. K., Jain, A., Taylor, G. A., & Chauhan, S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.11.018 · Cited by 238
Self-citationNakamura, S., Shigeyama, S., Minami, S., Shima, T., Akayama, S., Matsuda, T., Esposito, A., Napolitano, G., Kuma, A., Namba-Hamano, T., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00583-9 · Cited by 235
Detection and Clearance of Damaged Lysosomes by the Endo-Lysosomal Damage Response and Lysophagy
Papadopoulos, C., & Meyer, H. (2017) · Current Biology · doi:10.1016/j.cub.2017.11.012 · Cited by 230
Repair or Lysophagy: Dealing with Damaged Lysosomes
Papadopoulos, C., Kravic, B., & Meyer, H. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.08.010 · Cited by 212
Type-I-interferon-responsive microglia shape cortical development and behavior
Escoubas, C. C., Dorman, L. C., Nguyen, P. T., Lagares-Linares, C., Nakajo, H., Anderson, S. R., Barron, J. J., Wade, S. D., Cuevas, B., Vainchtein, I. D., et al. (2024) · Cell · doi:10.1016/j.cell.2024.02.020 · Cited by 179
Di Rienzo, M., Antonioli, M., Fusco, C., Liu, Y., Mari, M., Orhon, I., Refolo, G., Germani, F., Corazzari, M., Romagnoli, A., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau8857 · Cited by 107
Kumar, S., Jain, A., Choi, S. W., da Silva, G. P. D., Allers, L., Mudd, M. H., Peters, R. S., Anonsen, J. H., Rusten, T.-E., Lazarou, M., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0549-1 · Cited by 95
Self-citationAutophagy in metabolism and quality control: opposing, complementary or interlinked functions?
Deretic, V., & Kroemer, G. (2022) · Autophagy · doi:10.1080/15548627.2021.1933742 · Cited by 71
Self-citationIdentification of RING E3 pseudoligases in the TRIM protein family
(2025) · doi:10.1038/s41467-025-58807-1 · Cited by 20
‘Identification of RING E3 pseudoligases in the TRIM protein family’
Dudley-Fraser, J., Esposito, D., McPhie, K., Morley-Williams, C., Auchynnikava, T., & Rittinger, K. (2024) · doi:10.1101/2024.10.15.614675 · Cited by 1
Metadata
- Authors
- Chauhan, S., Kumar, S., Jain, A., Ponpuak, M., Mudd, M. H., Kimura, T., Choi, S. W., Peters, R., Mandell, M., Bruun, J.-A., Johansen, T., & Deretic, V.
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2016-10
- Volume
- 39
- Issue
- 1
- Pages
- 13-27
- ISSN
- 1534-5807 (ISSN-L)
- OpenAlex
- W2525950393
- Cited by
- 480
- References
- 11
- FWCI
- 25.90
- Type
- journal article
- Language
- en
- Open access
- bronze
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