Structure, lipid scrambling activity and role in autophagosome formation of ATG9A

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AMPK regulates phagophore-to-autophagosome maturation

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Morphology of Phagophore Precursors by Correlative Light-Electron Microscopy

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The mitophagy receptors BNIP3 and NIX mediate tight attachment and expansion of the isolation membrane to mitochondria

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The active zone protein Clarinet regulates synaptic sorting of ATG-9 and presynaptic autophagy

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A role for Vps13-mediated lipid transfer at the ER–endosome contact site in ESCRT-mediated sorting

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Molecular functions of autophagy adaptors upon ubiquitin-driven mitophagy

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ATG9A facilitates the closure of mammalian autophagosomes

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The human autophagy-initiating complexes ULK1C and PI3KC3-C1

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High-throughput imaging of ATG9A distribution as a diagnostic functional assay for adaptor protein complex 4-associated hereditary spastic paraplegia

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The Genetics of Autophagy in Multicellular Organisms

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Unraveling membrane properties at the organelle-level with LipidDyn

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ATG9B is a tissue-specific homotrimeric lipid scramblase that can compensate for ATG9A

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Quantitative Models of Lipid Transfer and Membrane Contact Formation

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Autophagy and mitophagy at the synapse and beyond: implications for learning, memory and neurological disorders

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“VTT”-Domain Proteins VMP1 and TMEM41B Function in Lipid Homeostasis Globally and Locally as ER Scramblases

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Molecular mechanisms of autophagy and implications in liver diseases

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RUSC2 and WDR47 oppositely regulate kinesin–1-dependent distribution of ATG9A to the cell periphery

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The autophagy protein ATG-9 regulates lysosome function and integrity

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The Role of WIPI2, ATG16L1 and ATG12-ATG5 in Selective and Nonselective Autophagy

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The emerging roles of autophagy in intestinal epithelial cells and its links to inflammatory bowel disease

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Toward a standard model for autophagosome biogenesis

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The role of lipid scramblases in regulating lipid distributions at cellular membranes

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Structural basis of closed groove scrambling by a TMEM16 protein

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The dual role of autophagy in suppressing and promoting hepatocellular carcinoma

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ATG9 Not Just an Autophagy Related Protein

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Dimerization-dependent membrane tethering by Atg23 is essential for yeast autophagy

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Secret of Atg9: lipid scramblase activity drives de novo autophagosome biogenesis

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Molecular Basis of Neuronal Autophagy in Ageing: Insights from Caenorhabditis elegans

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Links between autophagy and tissue mechanics

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Toxoplasma TgAtg8-TgAtg3 Interaction Primarily Contributes to Apicoplast Inheritance and Parasite Growth in Tachyzoite

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A neuroprotective role of Ufmylation through Atg9 in the aging brain of Drosophila

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Structural characterization of human urea transporters UT-A and UT-B and their inhibition

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Rim aperture of yeast autophagic membranes balances cargo inclusion with vesicle maturation

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ATG9A regulates proteostasis through reticulophagy receptors FAM134B and SEC62 and folding chaperones CALR and HSPB1

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Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy

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Sequestration of translation initiation factors in p62 condensates

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Organization of Presynaptic Autophagy-Related Processes

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Scramblases as Regulators of Proteolytic ADAM Function

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Autophagy-independent role of ATG9A vesicles as carriers for galectin-9 secretion

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Novel insights into autophagosome biogenesis revealed by cryo‐electron tomography

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The autophagy protein Atg9 functions in glia and contributes to parkinsonian symptoms in a Drosophila model of Parkinson’s disease

Yi, S., Wang, L., Ho, M. S., & Zhang, S. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382259 · Cited by 15

lncRNA TUG1 as Potential Novel Biomarker for Prognosis of Cardiovascular Diseases

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Established and emerging players in phospholipid scrambling: A structural perspective

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Early steps in the birth of four membrane-bound organelles—Peroxisomes, lipid droplets, lipoproteins, and autophagosomes

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ATG2A-mediated DAG transfer recruits DGAT2 for lipid droplet growth

Elhan, H., Damm, A., Korfhage, J. L., Álvarez, D., Zouiouich, M., Giordano, F., Vanni, S., Melia, T. J., & Thiam, A. R. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01689-0 · Cited by 17

Core principles of autophagy initiation mechanisms

Kotani, T., & Nakatogawa, H. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01752-4 · Cited by 15

Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway

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Iron regulatory protein two facilitates ferritinophagy and DNA damage/repair through guiding ATG9A trafficking

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S-palmitoylation modulates ATG2-dependent non-vesicular lipid transport during starvation-induced autophagy

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Autophagic and non-autophagic functions of the Saccharomyces cerevisiae PROPPINs Atg18, Atg21 and Hsv2

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Glycobiology of cellular expiry: Decrypting the role of glycan-lectin regulatory complex and therapeutic strategies focusing on cancer

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The dynamin Vps1 mediates Atg9 transport to the sites of autophagosome formation

Arlt, H., Raman, B., Filali-Mouncef, Y., Hu, Y. P., Leytens, A., Hardenberg, R., Guimarães, R. S., Kriegenburg, F., Mari, M. C., Rooij, I. I. S., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104712 · Cited by 12

Mechanisms of autophagosome formation

Fujioka, Y., & Noda, N. N. (2025) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.101.005 · Cited by 12

Any1 is a phospholipid scramblase involved in endosome biogenesis

Gao, J., Franzkoch, R., Rocha‐Roa, C., Psathaki, O. E., Hensel, M., Vanni, S., & Ungermann, C. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202410013 · Cited by 13

Atg9-centered multi-omics integration reveals new autophagy regulators inSaccharomyces cerevisiae

Peng, D., Ruan, C., Fu, S., He, C., Song, J.-Z., Li, H., Tu, Y., Tang, D., Yao, L., Lin, S., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1898749 · Cited by 11

Autophagy-associated immune dysregulation and hyperplasia in a patient with compound heterozygous mutations in ATG9A

Hu, G., Hauk, P. J., Zhang, N., Elsegeiny, W. A. W., Guardia, C. M. A., Kullas, A. L., Crosby, K., Deterding, R. R., Schedel, M., Reynolds, P. R., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2093028 · Cited by 12

The Organization and Function of the Phagophore-ER Membrane Contact Sites

Duarte, P. V., & Reggiori, F. (2023) · Contact · doi:10.1177/25152564231183898 · Cited by 12

Molecular and mesoscopic geometries in autophagosome generation. A review

Iriondo, M. N., Etxaniz, A., Antón, Z., Montes, L. R., & Alonso, A. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183731 · Cited by 12

Tweek-dependent formation of ER-PM contact sites enables astrocyte phagocytic function and remodeling of neuronsPreprint

Kang, Y., Jefferson, A., Sheehan, A. E., Torre, R. D. L., Jay, T. R., Chiao, L. J., Hulegaard, A. L., Corty, M. M., Baconguis, I., Zhou, Z., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.06.565932 · Cited by 10

Roles of Autophagy and Oxidative Stress in Cardiovascular Disease

Yun, H. R., Singh, M. K., Han, S., Ranbhise, J. S., Ha, J., Kim, S. S., & Kang, I. (2025) · Antioxidants · doi:10.3390/antiox14101263 · Cited by 13

Autophagy and the primary cilium in cell metabolism: What’s upstream?

Claude‐Taupin, A., Dupont, N., & Codogno, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1046248 · Cited by 11

In or out of the groove? Mechanisms of lipid scrambling by TMEM16 proteins

Feng, Z., Zanni, E. D., Alvarenga, O. E., Chakraborty, S., Rychlik, N., & Accardi, A. (2024) · Cell Calcium · doi:10.1016/j.ceca.2024.102896 · Cited by 11

Identification of a Proteomic Signature for Predicting Immunotherapy Response in Patients With Metastatic Non-Small Cell Lung Cancer

Mondelo‐Macía, P., García, J., León‐Mateos, L., Abalo, A., Bravo, S. B., Chantada‐Vázquez, M. D. P., Muinelo‐Romay, L., López‐López, R., Díaz‐Peña, R., & Dávila-Ibáñez, A. B. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100834 · Cited by 12

Autophagy in reproduction and pregnancy-associated diseases

Singh, A., Perez, M. L., Kirsanov, O., Padilla‐Banks, E., & Guardia, C. M. A. (2024) · iScience · doi:10.1016/j.isci.2024.111268 · Cited by 14

Membrane Contact Sites in Autophagy

Zwilling, E., & Reggiori, F. (2022) · Cells · doi:10.3390/cells11233813 · Cited by 11

How Membrane Contact Sites Shape the Phagophore

Capitanio, C., Bieber, A., & Wilfling, F. (2023) · Contact · doi:10.1177/25152564231162495 · Cited by 14

The role of the HORMA domain proteins ATG13 and ATG101 in initiating autophagosome biogenesis

Nguyen, A., & Faesen, A. C. (2023) · FEBS Letters · doi:10.1002/1873-3468.14717 · Cited by 11

Atg18 oligomer organization in assembled tubes and on lipid membrane scaffolds

Mann, D., Fromm, S. A., Martínez-Sánchez, A., Gopaldass, N., Choy, R., Mayer, A., & Sachse, C. (2023) · Nature Communications · doi:10.1038/s41467-023-43460-3 · Cited by 11

Recruitment of Atg1 to the phagophore by Atg8 orchestrates autophagy machineries

Song, J.-Z., Li, H., Yang, H., Liu, R., Zhang, W., He, T., Xie, M.-X., Chen, C., Cui, L., Wu, S., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01546-0 · Cited by 11

Epigenetic regulation of autophagy in coronavirus disease 2019 (COVID-19)

Behrouj, H., Vakili, O., Sadeghdoust, A., Aligolighasemabadi, N., Khalili, P., Zamani, M., & Mokarram, P. (2022) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2022.101264 · Cited by 11

Scramblases as Regulators of Autophagy and Lipid Homeostasis: Implications for NAFLD

Chen, A., Ding, W., & Ni, H. (2022) · Autophagy Reports · doi:10.1080/27694127.2022.2055724 · Cited by 11

The expanding role of Atg8

Hawkins, W. D., & Klionsky, D. J. (2021) · Autophagy · doi:10.1080/15548627.2021.1967566 · Cited by 10

MoMkk1 and MoAtg1 dichotomously regulating autophagy and pathogenicity through MoAtg9 phosphorylation in Magnaporthe oryzae

Kong, Y., Guo, P., Xu, J., Li, J., Wu, M., Zhang, Z., Wang, Y., Liu, X., Yang, L., Liu, M., et al. (2024) · mBio · doi:10.1128/mbio.03344-23 · Cited by 9

Phospholipid Supply for Autophagosome Biogenesis

Isola, D., & Elazar, Z. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168691 · Cited by 9

ATG9A vesicles are a subtype of intracellular nanovesicle

Fesenko, M., Moore, D. J., Ewbank, P., Courthold, E., & Royle, S. (2025) · Journal of Cell Science · doi:10.1242/jcs.263852 · Cited by 9

VPS13 and bridge-like lipid transporters, mechanisms, and mysteries

Swan, L. E. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1534061 · Cited by 11

Growing thin — How bulk lipid transport drives expansion of the autophagosome membrane but not of its lumen

Melia, T. J. (2023) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2023.102190 · Cited by 9

Faa1 membrane binding drives positive feedback in autophagosome biogenesis via fatty acid activation

Baumann, V., Achleitner, S., Tulli, S., Schuschnig, M., Klune, L., & Martens, S. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202309057 · Cited by 9

Visual detection of binary, ternary and quaternary protein interactions in fission yeast using a Pil1 co-tethering assay

Yu, Z.-Q., Liu, X., Zhao, D., Xu, D., & Du, L. (2021) · Journal of Cell Science · doi:10.1242/jcs.258774 · Cited by 9

Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblasePreprint

Jahn, H., Bartoš, L., Dearden, G. I., Dittman, J. S., Holthuis, J. C. M., Vácha, R., & Menon, A. K. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.17.512472 · Cited by 9

Sequencing of the ZMYND15 gene in a cohort of infertile Chinese men reveals novel mutations in patients with teratozoospermia

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PEX14 acts as a molecular link between optineurin and the autophagic machinery to induce pexophagy

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Primary cilium-dependent autophagy in the response to shear stress

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A method for the isolation and characterization of autophagic bodies from yeast provides a key tool to investigate cargos of autophagy

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Systematic Assessment of the Accuracy of Subunit Counting in Biomolecular Complexes Using Automated Single-Molecule Brightness Analysis

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Flip-Flop Promotion Mechanisms by Model Transmembrane Peptides

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Presynapses are mitophagy pit stops that prevent axon degenerationPreprint

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miRNA family miR-29 inhibits PINK1-PRKN dependent mitophagy via ATG9APreprint

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Tepsin binds LC3B to promote ATG9A trafficking and delivery

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Plant-specific mitochondrial fission machinery connects mitochondrial dynamics and mitophagosome formation for piecemeal mitophagy

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ATG9 vesicles comprise the seed membrane of mammalian autophagosomes

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The autophagy protein ATG9A enables lipid mobilization from lipid droplets

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ATG9A and ATG2A form a heteromeric complex essential for autophagosome formation.

Tooze, S. A. (2022) · Data Archiving and Networked Services (DANS) · doi:10.17632/rrfv4d7jnb

Secret of Atg9: lipid scramblase activity drives de novo autophagosome biogenesis

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