protein
Autophagy-related protein 2 homolog B
Gene
ATG2B
Organism
Homo sapiens(9606)
Length
2078 aa
Mass
232,763 Da
ATG2B (Autophagy-related protein 2 homolog B) is a lipid transfer protein essential for autophagosome biogenesis and lipid droplet regulation (UniProt: Q96BY7). It functions by tethering the isolation membrane to the endoplasmic reticulum and mediating phospholipid transfer from the ER to expanding autophagosomes, a process enhanced by the binding partner WDR45/WIPI4 (UniProt: Q96BY7). The protein plays a central role in autophagy, a critical cellular pathway for protein and organelle degradation.
ATG2B is expressed in human tissues and participates broadly in autophagy and lipid homeostasis pathways (UniProt: Q96BY7). No specific disease annotations are documented in the UniProt record for this protein.
In Alzheimer's Disease, ATG2B is significantly downregulated in post-mortem AD brain tissue compared to age-matched controls (mean log2FC: −0.6148; Chaparral AD proteomics). This reduction was observed across subcellular fractions in a TMT-labeled proteomics study, suggesting compromised autophagy capacity may contribute to AD pathology, as impaired autophagy is implicated in amyloid-β and tau accumulation.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
↓ Down in ADP3
-0.615
P2
not detected
S2
not detected
S3
not detected
Mean log₂FC across detected fractions: -0.6148 (1 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
Lipid transfer protein required for both autophagosome formation and regulation of lipid droplet morphology and dispersion (PubMed:22219374, PubMed:31721365). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (PubMed:22219374, PubMed:31721365). Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to the IM for membrane expansion (By similarity). Lipid transfer activity is enhanced by WDR45/WIPI4, which promotes ATG2B-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes (PubMed:31721365)
Sources
Last updated 5/8/2026, 6:28:41 AM
