Beclin-1 is the central scaffold subunit of class III phosphatidylinositol 3-kinase (PI3KC3/VPS34) complexes that generate phosphatidylinositol 3-phosphate (PI3P) for autophagosome biogenesis and endocytic trafficking. BECN1 forms two mutually exclusive complexes: PI3KC3-C1 (with ATG14L) for autophagosome nucleation, and PI3KC3-C2 (with UVRAG) for endosome maturation and endocytic trafficking. The protein contains an N-terminal BH3 domain (aa 108-127) that binds BCL2/BCL-XL to regulate autophagy, a coiled-coil domain (CCD; aa 144-269) for dimerization and partner binding, and a C-terminal BARA/ECD membrane-binding domain. BECN1 is a haploinsufficient tumor suppressor and is essential for autophagy initiation through its adapter function in assembling PI3KC3 complex components.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000045 autophagosome assembly | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 is essential for autophagosome assembly as the scaffold subunit of PI3KC3-C1 complex. This is a core function supported by extensive literature showing BECN1 with ATG14L, VPS34, and VPS15 generates PI3P required for phagophore nucleation (PMID:25891078, PMID:23878393). Reason: This is a core function of BECN1. The protein is the central scaffold of the PI3KC3-C1 complex that initiates autophagosome formation. The IBA annotation is based on phylogenetic inference including yeast Atg6/Vps30 and is strongly supported by direct experimental evidence. Supporting Evidence: PMID:25891078 IRGM interacts with ULK1 and Beclin 1 and promotes their co-assembly thus governing the formation of autophagy initiation complexes. PMID:23878393 Human beclin-1 and its yeast homologue, Atg6/Vps30, are scaffold proteins bound in a lipid kinase complex with multiple cellular functions, including autophagy. file:human/BECN1/BECN1-deep-research-falcon.md model: Edison Scientific Literature |
| GO:0000423 mitophagy | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 is specifically required for efficient mitophagy. Recent work shows Beclin-1 uniquely supports mitophagy by localizing to mitochondria-ER contact sites (MAMs) upon ULK1-Ser15 phosphorylation. Beclin-2 cannot substitute for this function (PMID:quiles2023, deep research). Reason: Core function. BECN1 is required for selective mitophagy through its localization to MAMs during mitochondrial depolarization. This is a specific autophagy-related function. Supporting Evidence: PMID:23878393 We identified a unique domain in beclin-1, conserved in the yeast homologue Atg6, which is involved in membrane association |
| GO:0030674 protein-macromolecule adaptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 functions as an adapter/scaffold to assemble the PI3KC3 complexes. It bridges VPS34/VPS15 with ATG14L or UVRAG to form functional lipid kinase complexes. This is its primary molecular function. Reason: Core molecular function. BECN1 is definitionally an adapter protein that scaffolds multiple components of the autophagy initiation machinery. The deep research confirms this is its primary molecular function. Supporting Evidence: PMID:25891078 IRGM interacts with ULK1 and Beclin 1 and promotes their co-assembly thus governing the formation of autophagy initiation complexes. |
| GO:0043548 phosphatidylinositol 3-kinase binding | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 directly binds VPS34 (PIK3C3), the catalytic subunit of the class III PI3K, through its coiled-coil and BARA domains. This interaction is essential for PI3KC3 complex function. Reason: Core molecular function. BECN1 binding to VPS34 is fundamental to its role in forming PI3KC3 complexes for autophagy and endocytic trafficking. Supporting Evidence: PMID:23878393 Human beclin-1 and its yeast homologue, Atg6/Vps30, are scaffold proteins bound in a lipid kinase complex |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 is a defining subunit of PI3KC3-C1, the autophagy-specific complex containing BECN1-VPS34-VPS15-ATG14L. This complex generates PI3P for autophagosome nucleation. Reason: Core localization. BECN1 is an obligate component of PI3KC3-C1, the autophagy initiation complex. Supporting Evidence: PMID:25891078 IRGM interacts with ULK1 and Beclin 1 and promotes their co-assembly |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 is a defining subunit of PI3KC3-C2, the endocytic trafficking complex containing BECN1-VPS34-VPS15-UVRAG. This complex is involved in endosome maturation and receptor trafficking. Reason: Core localization. BECN1 is an obligate component of PI3KC3-C2. The deep research confirms PI3KC3-C2 (UVRAG-containing) is involved in endosome maturation and receptor sorting. |
| GO:0000407 phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 localizes to the phagophore assembly site (PAS) as part of the PI3KC3-C1 complex to initiate autophagosome formation. This is consistent with its function in autophagy initiation. Reason: Core localization for autophagy function. The PI3KC3-C1 complex localizes to PAS. |
| GO:0006995 cellular response to nitrogen starvation | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 is activated during nitrogen/amino acid starvation to induce autophagy. This is conserved from yeast (Atg6/Vps30) through humans. Reason: Core function. Autophagy induction in response to nutrient starvation is a fundamental BECN1 function. |
| GO:0045324 late endosome to vacuole transport | IBA GO_REF:0000033 | ACCEPT | Summary: BECN1 in the PI3KC3-C2 complex (with UVRAG) regulates endosome maturation including early-to-late endosome transport and late endosome-lysosome fusion. Reason: Represents the endocytic trafficking function of BECN1 via PI3KC3-C2 complex. This is distinct from but related to autophagy. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: BECN1 has been detected in the nucleus in some studies. UniProt annotation based on subcellular location vocabulary mapping. Reason: Not a primary localization. BECN1 may transit through nucleus but its functional localization is cytoplasmic/membrane-associated. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: BECN1 localizes to the cytoplasm where it assembles PI3KC3 complexes. This is consistent with experimental data. Reason: Core localization. The cytoplasm is where BECN1 assembles with VPS34 and other components. |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: BECN1 localizes to mitochondria-ER contact sites (MAMs) during mitophagy, where it promotes selective degradation of damaged mitochondria. Reason: Supports mitophagy function. BECN1 relocates to MAMs during mitochondrial depolarization. |
| GO:0005768 endosome | IEA GO_REF:0000044 | ACCEPT | Summary: BECN1 localizes to endosomes as part of PI3KC3-C2 complex function in endocytic trafficking. Reason: Consistent with PI3KC3-C2 function in endosome maturation. |
| GO:0005776 autophagosome | IEA GO_REF:0000120 | ACCEPT | Summary: BECN1 localizes to autophagosomes during their formation as part of PI3KC3-C1. Reason: Core localization for autophagy function. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: BECN1 associates with ER membrane where autophagosome nucleation occurs. The ER is a major membrane source for autophagosome formation. Reason: Consistent with autophagosome nucleation occurring at ER membranes. |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | ACCEPT | Summary: BECN1 localizes to Golgi/TGN membranes, particularly the PI3KC3-C2 complex which functions in TGN-proximal trafficking. Reason: Consistent with PI3KC3-C2 function in membrane trafficking. |
| GO:0006897 endocytosis | IEA GO_REF:0000043 | ACCEPT | Summary: BECN1 in PI3KC3-C2 complex regulates endocytic trafficking, including receptor sorting and endosome maturation. This is a non-autophagy function. Reason: Represents PI3KC3-C2 function. Not over-annotation - BECN1 has demonstrated roles in endocytic trafficking independent of autophagy. |
| GO:0006914 autophagy | IEA GO_REF:0000120 | ACCEPT | Summary: BECN1 is a central regulator of autophagy as the scaffold of PI3KC3-C1 complex. Reason: Core function. Autophagy is the primary biological process for BECN1. |
| GO:0006915 apoptotic process | IEA GO_REF:0000043 | MARK AS OVER ANNOTATED | Summary: This annotation derives from UniProt keyword mapping. While BECN1 interacts with BCL2 family members via its BH3 domain, this interaction serves to REGULATE AUTOPHAGY, not apoptosis. BCL2/BCL-XL sequester BECN1 to inhibit autophagy; competitive displacement releases BECN1 for autophagy induction. The BH3 domain of BECN1 is atypical and has been "designed to induce autophagy by disrupting the Bcl-2-Beclin1 complex without inducing cell death" (PMID:19273585). BECN1 is not an apoptosis effector. Reason: OVER-ANNOTATION. The BCL2 interaction is for autophagy regulation, not apoptosis. BECN1 contains a BH3-like domain but this domain functions in autophagy regulation by allowing BCL2 to sequester BECN1. When BH3-only proteins compete for BCL2 binding, BECN1 is released to activate autophagy - this is NOT an apoptotic function. The deep research clearly states BECN1's core function is autophagy/PI3KC3 scaffold, and the BCL2 binding is regulatory crosstalk. Supporting Evidence: PMID:19273585 we propose a model in which the atypical BH3 domains of hypoxia-induced BNIP3/BNIP3L have been designed to induce autophagy by disrupting the Bcl-2-Beclin1 complex without inducing cell death PMID:17446862 The anti-apoptotic proteins Bcl-2 and Bcl-X(L) bind and inhibit Beclin-1, an essential mediator of autophagy... BH3-only proteins and pharmacological BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin-1 and Bcl-2 or Bcl-X(L). |
| GO:0010008 endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: BECN1 localizes to endosome membranes as part of PI3KC3-C2 function. Reason: Consistent with endocytic trafficking function. |
| GO:0031410 cytoplasmic vesicle | IEA GO_REF:0000120 | ACCEPT | Summary: BECN1 associates with various cytoplasmic vesicles including autophagosomes and endosomes. Reason: General but accurate. BECN1 functions on multiple vesicle types. |
| GO:0031966 mitochondrial membrane | IEA GO_REF:0000044 | ACCEPT | Summary: BECN1 localizes to mitochondrial membranes, particularly MAMs during mitophagy. Reason: Supports mitophagy function. |
| GO:0032801 receptor catabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: BECN1 in PI3KC3-C2 complex is involved in receptor trafficking including EGFR sorting. The deep research mentions "receptor sorting (e.g., EGFR, TFR1)". Reason: Consistent with PI3KC3-C2 function in endocytic trafficking and receptor turnover. |
| GO:0051301 cell division | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: BECN1 has been implicated in cytokinesis regulation through PI3KC3-C2 function. This represents a non-autophagy function. Reason: Secondary function. BECN1 has been shown to regulate cytokinesis (PMID:20208530, PMID:20643123) but this is not its primary function. |
| GO:0051607 defense response to virus | IEA GO_REF:0000043 | ACCEPT | Summary: BECN1 was originally discovered as protective against Sindbis virus encephalitis (PMID:9765397). Autophagy plays a role in antiviral defense, and many viruses target BECN1 to evade autophagy. Reason: Legitimate function. BECN1 plays a role in antiviral autophagy (xenophagy), and the original discovery paper demonstrated its protective role against viral infection. Supporting Evidence: PMID:9765397 These findings demonstrate that Beclin is a novel Bcl-2-interacting cellular protein that may play a role in antiviral host defense. |
| GO:0005515 protein binding | IPI PMID:17446862 Functional and physical interaction between Bcl-X(L) and a B... | REMOVE | Summary: This paper demonstrated physical interaction between BECN1 BH3 domain and BCL2/BCL-XL using multiple methods. The interaction regulates autophagy - BCL-XL inhibits BECN1-dependent autophagy through this binding. Reason: Generic protein binding is uninformative. The specific binding activity (BCL2/BCL-XL binding) is captured in other more specific annotations. Should be annotated to a more specific MF term if appropriate. Supporting Evidence: PMID:17446862 The anti-apoptotic proteins Bcl-2 and Bcl-X(L) bind and inhibit Beclin-1, an essential mediator of autophagy |
| GO:0005515 protein binding | IPI PMID:19050071 Identification of Barkor as a mammalian autophagy-specific f... | REMOVE | Summary: This paper identified ATG14 (Barkor) as a BECN1-binding protein that directs BECN1/VPS34 to autophagosome formation sites. Core autophagy complex formation. Reason: Generic protein binding is uninformative. The functional significance (autophagy complex formation) is captured in other annotations. Supporting Evidence: PMID:19050071 Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. |
| GO:0005515 protein binding | IPI PMID:19180116 DAP-kinase-mediated phosphorylation on the BH3 domain of bec... | REMOVE | Summary: This paper showed DAPK1 phosphorylates BECN1 at Thr119 in the BH3 domain to promote dissociation from BCL-XL and induce autophagy. Reason: Generic protein binding is uninformative. The interaction with DAPK1 is functionally relevant to autophagy regulation. Supporting Evidence: PMID:19180116 DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. |
| GO:0005515 protein binding | IPI PMID:19959994 The IKK complex contributes to the induction of autophagy. | REMOVE | Summary: IKK complex interaction study. Protein binding annotation is too generic. Reason: Generic protein binding term is uninformative for understanding gene function. Supporting Evidence: PMID:19959994 The IKK complex contributes to the induction of autophagy. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: Network analysis of human autophagy system interactions. Reason: Generic protein binding term is uninformative for understanding gene function. Supporting Evidence: PMID:20562859 Network organization of the human autophagy system. |
| GO:0005515 protein binding | IPI PMID:20638385 Interaction of Beclin 1 with survivin regulates sensitivity ... | REMOVE | Summary: This paper studied BECN1-survivin interaction in glioma cells regarding TRAIL-induced apoptosis. Reason: Generic protein binding. Also relates to apoptosis context which is not core BECN1 function. Supporting Evidence: PMID:20638385 Epub 2010 Jul 16. Interaction of Beclin 1 with survivin regulates sensitivity of human glioma cells to TRAIL-induced apoptosis. |
| GO:0005515 protein binding | IPI PMID:20819940 Endogenous HMGB1 regulates autophagy. | REMOVE | Summary: HMGB1-BECN1 interaction study showing HMGB1 regulates autophagy through BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:20819940 Endogenous HMGB1 regulates autophagy. |
| GO:0005515 protein binding | IPI PMID:21062745 The RUN domain of rubicon is important for hVps34 binding, l... | REMOVE | Summary: Rubicon RUN domain interaction with VPS34 and BECN1 complex regulation. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:21062745 Nov 9. The RUN domain of rubicon is important for hVps34 binding, lipid kinase inhibition, and autophagy suppression. |
| GO:0005515 protein binding | IPI PMID:21139567 MCL-1 is a stress sensor that regulates autophagy in a devel... | REMOVE | Summary: MCL-1 interaction with BECN1 to regulate autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:21139567 MCL-1 is a stress sensor that regulates autophagy in a developmentally regulated manner. |
| GO:0005515 protein binding | IPI PMID:21241894 RalB and the exocyst mediate the cellular starvation respons... | REMOVE | Summary: RalB and exocyst complex mediate autophagy through BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:21241894 RalB and the exocyst mediate the cellular starvation response by direct activation of autophagosome assembly. |
| GO:0005515 protein binding | IPI PMID:21358617 Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy. | REMOVE | Summary: Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy through BECN1 interaction. This paper demonstrates BCL2-BECN1 interaction at mitochondria regulates autophagy. Reason: Generic protein binding. The BCL2 interaction is for autophagy regulation. Supporting Evidence: PMID:21358617 Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy. |
| GO:0005515 protein binding | IPI PMID:21597469 UV irradiation resistance-associated gene suppresses apoptos... | REMOVE | Summary: UVRAG suppresses apoptosis by interfering with BAX activation. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:21597469 UV irradiation resistance-associated gene suppresses apoptosis by interfering with BAX activation. |
| GO:0005515 protein binding | IPI PMID:22028648 An integrated approach to elucidate the intra-viral and vira... | REMOVE | Summary: Gamma-herpesvirus protein interactome study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:22028648 2011 Oct 20. An integrated approach to elucidate the intra-viral and viral-cellular protein interaction networks of a gamma-herpesvirus. |
| GO:0005515 protein binding | IPI PMID:22081109 Inhibition of autophagy by TAB2 and TAB3. | REMOVE | Summary: TAB2/TAB3 inhibit autophagy through BECN1 interaction. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:22081109 Inhibition of autophagy by TAB2 and TAB3. |
| GO:0005515 protein binding | IPI PMID:22493499 Receptor signaling lymphocyte-activation molecule family 1 (... | REMOVE | Summary: SLAMF1 recruits BECN1-VPS34-UVRAG complex for NOX2 regulation. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:22493499 2012 Apr 9. Receptor signaling lymphocyte-activation molecule family 1 (Slamf1) regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-associated gene (UVRAG) complex. |
| GO:0005515 protein binding | IPI PMID:23112296 Akt-mediated regulation of autophagy and tumorigenesis throu... | REMOVE | Summary: Akt-mediated phosphorylation of BECN1 regulates autophagy and tumorigenesis. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23112296 Oct 25. Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation. |
| GO:0005515 protein binding | IPI PMID:23197835 Autophagosomes induced by a bacterial Beclin 1 binding prote... | REMOVE | Summary: Bacterial Beclin 1 binding protein study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23197835 Autophagosomes induced by a bacterial Beclin 1 binding protein facilitate obligatory intracellular infection. |
| GO:0005515 protein binding | IPI PMID:23316280 The VMP1-Beclin 1 interaction regulates autophagy induction. | REMOVE | Summary: VMP1-BECN1 interaction regulates autophagy induction. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23316280 The VMP1-Beclin 1 interaction regulates autophagy induction. |
| GO:0005515 protein binding | IPI PMID:23332761 Differential regulation of distinct Vps34 complexes by AMPK ... | REMOVE | Summary: Differential regulation of VPS34 complexes by AMPK. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23332761 Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy. |
| GO:0005515 protein binding | IPI PMID:23364696 Identification of a candidate therapeutic autophagy-inducing... | REMOVE | Summary: Identification of autophagy-inducing peptide derived from BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23364696 Identification of a candidate therapeutic autophagy-inducing peptide. |
| GO:0005515 protein binding | IPI PMID:23478334 Beclin-1 is required for chromosome congression and proper o... | REMOVE | Summary: BECN1 is required for chromosome congression and kinetochore assembly. This is a non-autophagy function. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23478334 Beclin-1 is required for chromosome congression and proper outer kinetochore assembly. |
| GO:0005515 protein binding | IPI PMID:23541952 Control of autophagic cell death by caspase-10 in multiple m... | REMOVE | Summary: Control of autophagic cell death by caspase-10 in multiple myeloma. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23541952 2013 Mar 28. Control of autophagic cell death by caspase-10 in multiple myeloma. |
| GO:0005515 protein binding | IPI PMID:23954414 Beclin 2 functions in autophagy, degradation of G protein-co... | REMOVE | Summary: Beclin 2 functions study - comparison with BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23954414 Aug 15. Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism. |
| GO:0005515 protein binding | IPI PMID:23974797 WASH inhibits autophagy through suppression of Beclin 1 ubiq... | REMOVE | Summary: WASH inhibits autophagy through suppression of BECN1 ubiquitination. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23974797 WASH inhibits autophagy through suppression of Beclin 1 ubiquitination. |
| GO:0005515 protein binding | IPI PMID:24034250 EGFR-mediated Beclin 1 phosphorylation in autophagy suppress... | REMOVE | Summary: EGFR-mediated BECN1 phosphorylation suppresses autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24034250 EGFR-mediated Beclin 1 phosphorylation in autophagy suppression, tumor progression, and tumor chemoresistance. |
| GO:0005515 protein binding | IPI PMID:24056303 PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and A... | REMOVE | Summary: UVRAG coordinates Golgi-ER retrograde transport with BECN1 complex. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24056303 PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex. |
| GO:0005515 protein binding | IPI PMID:24349490 Rab39a interacts with phosphatidylinositol 3-kinase and nega... | REMOVE | Summary: Rab39a negatively regulates autophagy through BECN1 interaction. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24349490 eCollection 2013. Rab39a interacts with phosphatidylinositol 3-kinase and negatively regulates autophagy induced by lipopolysaccharide stimulation in macrophages. |
| GO:0005515 protein binding | IPI PMID:24443581 Targeting Ξ³-herpesvirus 68 Bcl-2-mediated down-regulation of... | REMOVE | Summary: Gamma-herpesvirus BCL-2 targeting of autophagy through BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24443581 2014 Jan 17. Targeting Ξ³-herpesvirus 68 Bcl-2-mediated down-regulation of autophagy. |
| GO:0005515 protein binding | IPI PMID:24472739 Decorin activates AMPK, an energy sensor kinase, to induce a... | REMOVE | Summary: Decorin activates AMPK to induce autophagy through BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24472739 Jan 26. Decorin activates AMPK, an energy sensor kinase, to induce autophagy in endothelial cells. |
| GO:0005515 protein binding | IPI PMID:24785657 NRBF2 regulates macroautophagy as a component of Vps34 Compl... | REMOVE | Summary: NRBF2 regulates macroautophagy as component of VPS34 complex I. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24785657 NRBF2 regulates macroautophagy as a component of Vps34 Complex I. |
| GO:0005515 protein binding | IPI PMID:25311841 Coronavirus membrane-associated papain-like proteases induce... | REMOVE | Summary: Coronavirus papain-like proteases interact with BECN1 to regulate autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:25311841 Oct 15. Coronavirus membrane-associated papain-like proteases induce autophagy through interacting with Beclin1 to negatively regulate antiviral innate immunity. |
| GO:0005515 protein binding | IPI PMID:25438055 AMBRA1 links autophagy to cell proliferation and tumorigenes... | REMOVE | Summary: AMBRA1 links autophagy to cell proliferation through BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:25438055 AMBRA1 links autophagy to cell proliferation and tumorigenesis by promoting c-Myc dephosphorylation and degradation. |
| GO:0005515 protein binding | IPI PMID:25490155 Architecture and dynamics of the autophagic phosphatidylinos... | REMOVE | Summary: Architecture of autophagic PI3K complex - structural study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:25490155 Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex. |
| GO:0005515 protein binding | IPI PMID:25594178 A kinase-independent role for EGF receptor in autophagy init... | REMOVE | Summary: Kinase-independent role for EGFR in autophagy initiation. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:25594178 A kinase-independent role for EGF receptor in autophagy initiation. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Human interactome study - high-throughput. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:26496610 Oct 22. A human interactome in three quantitative dimensions organized by stoichiometries and abundances. |
| GO:0005515 protein binding | IPI PMID:26783301 Negative regulation of phosphatidylinositol 3-phosphate leve... | REMOVE | Summary: PI3P regulation in endosome conversion involving BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:26783301 Negative regulation of phosphatidylinositol 3-phosphate levels in early-to-late endosome conversion. |
| GO:0005515 protein binding | IPI PMID:28445460 Polyglutamine tracts regulate beclin 1-dependent autophagy. | REMOVE | Summary: Polyglutamine tracts regulate BECN1-dependent autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:28445460 Polyglutamine tracts regulate beclin 1-dependent autophagy. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Architecture of human interactome - high-throughput study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:28514442 Architecture of the human interactome defines protein communities and disease networks. |
| GO:0005515 protein binding | IPI PMID:29849149 Disruption of the beclin 1-BCL2 autophagy regulatory complex... | REMOVE | Summary: Disruption of BECN1-BCL2 complex promotes longevity in mice. Key study showing BCL2-BECN1 interaction regulates autophagy and lifespan. Reason: Generic protein binding term is uninformative. The BCL2 interaction is for autophagy regulation. Supporting Evidence: PMID:29849149 May 30. Disruption of the beclin 1-BCL2 autophagy regulatory complex promotes longevity in mice. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Reference map of human binary protein interactome. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:32296183 Apr 8. A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Interactome mapping in neurodegenerative disease proteins. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:33422265 ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-m... | REMOVE | Summary: SARS-CoV-2 ORF3a blocks autophagosome-lysosome fusion. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:33422265 Epub 2020 Dec 16. ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated assembly of the SNARE complex required for autolysosome formation. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Dual proteome-scale networks study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:33961781 2021 May 6. Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005515 protein binding | IPI PMID:34386498 ORF3a-Mediated Incomplete Autophagy Facilitates Severe Acute... | REMOVE | Summary: SARS-CoV-2 ORF3a-mediated incomplete autophagy study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:34386498 eCollection 2021. ORF3a-Mediated Incomplete Autophagy Facilitates Severe Acute Respiratory Syndrome Coronavirus-2 Replication. |
| GO:0005515 protein binding | IPI PMID:34524948 Global Proximity Interactome of the Human Macroautophagy Pat... | REMOVE | Summary: Global proximity interactome of human macroautophagy pathway. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:34524948 2021 Sep 15. Global Proximity Interactome of the Human Macroautophagy Pathway. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: OpenCell endogenous tagging study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:35271311 2022 Mar 11. OpenCell: Endogenous tagging for the cartography of human cellular organization. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: Mutation-directed neo-protein-protein interactions in cancer. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:35512704 2022 May 4. Systematic discovery of mutation-directed neo-protein-protein interactions in cancer. |
| GO:0005515 protein binding | IPI PMID:38182563 GRB2 is a BECN1 interacting protein that regulates autophagy... | REMOVE | Summary: GRB2 is a BECN1 interacting protein that regulates autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:38182563 GRB2 is a BECN1 interacting protein that regulates autophagy. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Multimodal cell maps study. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:40205054 Apr 9. Multimodal cell maps as a foundation for structural and functional genomics. |
| GO:0000045 autophagosome assembly | IEA GO_REF:0000120 | ACCEPT | Summary: Duplicate of IBA annotation. Core autophagy function. Reason: Core function - duplicates IBA annotation. |
| GO:0001666 response to hypoxia | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Autophagy is induced during hypoxia, and BECN1 participates in this response. BNIP3/BNIP3L displace BCL2 from BECN1 to activate autophagy under hypoxia. Reason: Secondary function. BECN1 participates in hypoxia-induced autophagy through the BNIP3/BNIP3L-BCL2-BECN1 pathway (PMID:19273585). Supporting Evidence: PMID:19273585 we propose a model in which the atypical BH3 domains of hypoxia-induced BNIP3/BNIP3L have been designed to induce autophagy by disrupting the Bcl-2-Beclin1 complex |
| GO:0005802 trans-Golgi network | IEA GO_REF:0000120 | ACCEPT | Summary: BECN1 localizes to TGN as part of PI3KC3-C2 function. Reason: Consistent with endocytic trafficking function. |
| GO:0007254 JNK cascade | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: JNK phosphorylates BCL2 to release BECN1 for autophagy activation. This represents regulatory input to BECN1. Reason: BECN1 is downstream of JNK signaling through BCL2 phosphorylation. Not direct JNK cascade component. |
| GO:0007623 circadian rhythm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Autophagy is regulated by circadian rhythm; this annotation likely reflects circadian regulation of autophagy genes including BECN1. Reason: Secondary/regulatory. BECN1 expression may be circadian-regulated but circadian rhythm is not its core function. |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Autophagy responds to xenobiotic stress; BECN1 participates in this. Reason: Secondary. Autophagy is a general stress response mechanism. |
| GO:0010040 response to iron(II) ion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Iron can regulate autophagy; this is likely through general stress response. Reason: Secondary stress response annotation. |
| GO:0010288 response to lead ion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Heavy metal stress induces autophagy. Reason: Secondary stress response annotation. |
| GO:0010508 positive regulation of autophagy | IEA GO_REF:0000107 | ACCEPT | Summary: BECN1 is a positive regulator of autophagy as scaffold of PI3KC3-C1. Reason: Core function. BECN1 positively regulates autophagy initiation. |
| GO:0016236 macroautophagy | IEA GO_REF:0000107 | ACCEPT | Summary: BECN1 is essential for macroautophagy as scaffold of PI3KC3-C1. Reason: Core function. Macroautophagy is the primary type of autophagy BECN1 regulates. |
| GO:0030425 dendrite | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BECN1 may localize to dendrites in neurons. Neuronal autophagy is important for synaptic function. Reason: Cell type-specific localization. Not core function. |
| GO:0030674 protein-macromolecule adaptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Duplicate annotation - BECN1 has adapter/scaffold function. Reason: Core molecular function - duplicates IBA annotation. |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000107 | ACCEPT | Summary: BECN1 is regulated by ubiquitination and binds E3 ligases like NEDD4. Reason: Regulatory interaction. BECN1 is ubiquitinated by multiple E3 ligases to regulate its stability and activity. |
| GO:0031667 response to nutrient levels | IEA GO_REF:0000107 | ACCEPT | Summary: BECN1-dependent autophagy is activated in response to nutrient deprivation. Reason: Core function. Nutrient starvation is a primary trigger for BECN1-dependent autophagy. |
| GO:0032991 protein-containing complex | IEA GO_REF:0000107 | MODIFY | Summary: BECN1 is part of PI3KC3 complexes. Too generic. Reason: Should be more specific - annotated to PI3KC3 complex terms instead. Proposed replacements: phosphatidylinositol 3-kinase complex, class III |
| GO:0033197 response to vitamin E | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Vitamin E can affect autophagy. Indirect effect. Reason: Secondary/indirect effect. |
| GO:0034198 cellular response to amino acid starvation | IEA GO_REF:0000107 | ACCEPT | Summary: BECN1-dependent autophagy is induced by amino acid starvation. Reason: Core function. Amino acid starvation is a primary trigger for autophagy. |
| GO:0035032 phosphatidylinositol 3-kinase complex, class III | IEA GO_REF:0000107 | ACCEPT | Summary: BECN1 is a core component of PI3KC3 complexes. Reason: Core localization. BECN1 is an obligate subunit of PI3KC3. |
| GO:0038066 p38MAPK cascade | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: p38 MAPK can regulate autophagy; BECN1 may be downstream. Reason: Secondary regulatory input to autophagy. |
| GO:0042149 cellular response to glucose starvation | IEA GO_REF:0000107 | ACCEPT | Summary: Glucose starvation induces autophagy through AMPK-BECN1 pathway. Reason: Core function. Metabolic stress triggers autophagy. |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BECN1 can homodimerize through its coiled-coil domain. However, functional complexes involve heterodimerization with ATG14L or UVRAG. Reason: The coiled-coil domain can mediate homodimerization, but this is less functionally relevant than heterodimerization. |
| GO:0043066 negative regulation of apoptotic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This annotation likely reflects that autophagy can be anti-apoptotic by removing damaged mitochondria. However, this is an indirect effect through autophagy, not direct anti-apoptotic activity. Reason: OVER-ANNOTATION. BECN1 is an autophagy protein, not an apoptosis regulator. Any anti-apoptotic effect is secondary to its autophagy function. The BCL2 binding is for autophagy regulation, not apoptosis regulation. |
| GO:0043652 engulfment of apoptotic cell | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: LC3-associated phagocytosis (LAP) involves BECN1 complexes for clearance of apoptotic cells. This is a non-canonical autophagy function. Reason: Secondary function. LAP uses autophagy machinery for phagocytic clearance. |
| GO:0045335 phagocytic vesicle | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BECN1 participates in LC3-associated phagocytosis. Reason: Secondary function related to LAP. |
| GO:0060395 SMAD protein signal transduction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Connection to SMAD signaling is likely indirect through autophagy-TGFbeta crosstalk. Reason: Indirect/secondary effect. |
| GO:0062029 positive regulation of stress granule assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Stress granules and autophagy are connected processes. Reason: Secondary/indirect connection. |
| GO:0070301 cellular response to hydrogen peroxide | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Oxidative stress induces autophagy. Reason: Secondary stress response. |
| GO:0071275 cellular response to aluminum ion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Heavy metal stress can induce autophagy. Reason: Secondary stress response. |
| GO:0071280 cellular response to copper ion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Metal ion stress and autophagy. Reason: Secondary stress response. |
| GO:0071364 cellular response to epidermal growth factor stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR phosphorylates BECN1 to suppress autophagy. This is a regulatory input. Reason: Regulatory input. EGFR-mediated phosphorylation suppresses BECN1 activity. |
| GO:0090650 cellular response to oxygen-glucose deprivation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Metabolic stress induces autophagy. Reason: Secondary stress response function. |
| GO:1905672 negative regulation of lysosome organization | IEA GO_REF:0000107 | UNDECIDED | Summary: BECN1 affects lysosome function through autophagy pathway. Reason: Unclear annotation - need more evidence for this specific function. |
| GO:2000786 positive regulation of autophagosome assembly | IEA GO_REF:0000107 | ACCEPT | Summary: BECN1 positively regulates autophagosome assembly as scaffold of PI3KC3-C1. Reason: Core function. |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This annotation is problematic. BECN1's connection to apoptosis is through its interaction with BCL2 family, but this interaction REGULATES AUTOPHAGY, not apoptosis. BECN1 is NOT a positive regulator of apoptosis. Reason: OVER-ANNOTATION. BECN1 is NOT an apoptosis regulator. The BCL2 binding domain functions in autophagy regulation. Any effect on apoptosis is indirect through autophagy-apoptosis crosstalk, not direct regulation of apoptotic pathways. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: BECN1 localizes to cytosol based on immunofluorescence. Reason: Core localization. |
| GO:0016604 nuclear body | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: BECN1 detected in nuclear bodies by immunofluorescence. Reason: Not a primary localization. May represent minor pool. |
| GO:0016236 macroautophagy | NAS PMID:40442316 Structure and activation of the human autophagy-initiating U... | ACCEPT | Summary: Recent structural study of ULK1C:PI3KC3-C1 supercomplex confirms BECN1 role in macroautophagy. Reason: Core function confirmed by structural studies. Supporting Evidence: PMID:40442316 Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex. |
| GO:0006622 protein targeting to lysosome | NAS PMID:16467569 Regulation of membrane traffic by phosphoinositide 3-kinases... | KEEP AS NON CORE | Summary: BECN1 in PI3KC3-C2 regulates trafficking to lysosome. Reason: Related to PI3KC3-C2 endocytic trafficking function. Supporting Evidence: PMID:16467569 Regulation of membrane traffic by phosphoinositide 3-kinases. |
| GO:0010506 regulation of autophagy | IDA PMID:16799551 Autophagic and tumour suppressor activity of a novel Beclin1... | ACCEPT | Summary: This paper identified UVRAG as BECN1-binding protein that regulates autophagy. Demonstrates BECN1's role in autophagy regulation. Reason: Core function. Supporting Evidence: PMID:16799551 UVRAG, a tumour suppressor candidate... associates with the Beclin1-Bcl-2-PI(3)KC3 multiprotein complex, where UVRAG and Beclin1 interdependently induce autophagy |
| GO:0016241 regulation of macroautophagy | IDA PMID:10625637 Distinct classes of phosphatidylinositol 3'-kinases are invo... | ACCEPT | Summary: Foundational paper showing class III PI3K (VPS34) is required for macroautophagy. BECN1 as VPS34 scaffold regulates this process. Reason: Core function. Supporting Evidence: PMID:10625637 an increase in the class III PI3K product (phosphatidylinositol 3-phosphate)... stimulates macroautophagy |
| GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process | IDA PMID:8999962 Characterization of p150, an adaptor protein for the human p... | ACCEPT | Summary: BECN1 as scaffold of VPS34 complex enables PI3P synthesis. VPS34 is the lipid kinase; BECN1 is the adapter. Reason: Core function. BECN1 enables PI3P synthesis by scaffolding VPS34 complex. Supporting Evidence: PMID:8999962 Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. |
| GO:0045022 early endosome to late endosome transport | IDA PMID:14617358 Human VPS34 and p150 are Rab7 interacting partners. | ACCEPT | Summary: VPS34 and BECN1 interact with Rab7 for endosome maturation. Reason: Related to PI3KC3-C2 endocytic trafficking function. Supporting Evidence: PMID:14617358 Human VPS34 and p150 are Rab7 interacting partners. |
| GO:0097352 autophagosome maturation | IDA PMID:10625637 Distinct classes of phosphatidylinositol 3'-kinases are invo... | ACCEPT | Summary: PI3KC3 regulates autophagosome maturation in addition to initiation. Reason: Core autophagy function. Supporting Evidence: PMID:10625637 Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9837231 | ACCEPT | Summary: Reactome annotation for ISGylation of BECN1 in cytosol. Reason: Core localization. |
| GO:0000423 mitophagy | IMP PMID:25215947 AMBRA1 is able to induce mitophagy via LC3 binding, regardle... | ACCEPT | Summary: AMBRA1 can induce mitophagy via LC3 binding - involves BECN1 complex. Reason: Core function - mitophagy. Supporting Evidence: PMID:25215947 Sep 12. AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1. |
| GO:0000045 autophagosome assembly | IDA PMID:25891078 IRGM governs the core autophagy machinery to conduct antimic... | ACCEPT | Summary: IRGM governs autophagy machinery by assembling ULK1 and BECN1 complexes. Reason: Core function. Supporting Evidence: PMID:25891078 IRGM interacts with ULK1 and Beclin 1 and promotes their co-assembly thus governing the formation of autophagy initiation complexes |
| GO:0030674 protein-macromolecule adaptor activity | IDA PMID:25891078 IRGM governs the core autophagy machinery to conduct antimic... | ACCEPT | Summary: Direct demonstration of BECN1's adapter function in assembling autophagy complexes. Reason: Core molecular function. Supporting Evidence: PMID:25891078 IRGM interacts with ULK1 and Beclin 1 and promotes their co-assembly |
| GO:0002753 cytoplasmic pattern recognition receptor signaling pathway | IDA PMID:34796041 Hepatitis B virus X Protein Promotes Liver Cancer Progressio... | KEEP AS NON CORE | Summary: BECN1 links TLR4 signaling to autophagy in liver cancer context. Reason: Represents autophagy response to PRR signaling. Not core function. Supporting Evidence: PMID:34796041 2021 Oct. Hepatitis B virus X Protein Promotes Liver Cancer Progression through Autophagy Induction in Response to TLR4 Stimulation. |
| GO:0060090 molecular adaptor activity | IDA PMID:34796041 Hepatitis B virus X Protein Promotes Liver Cancer Progressio... | ACCEPT | Summary: BECN1 has molecular adapter activity - core function. Reason: Core molecular function. Supporting Evidence: PMID:34796041 2021 Oct. Hepatitis B virus X Protein Promotes Liver Cancer Progression through Autophagy Induction in Response to TLR4 Stimulation. |
| GO:0043069 negative regulation of programmed cell death | IMP PMID:19273585 Hypoxia-induced autophagy is mediated through hypoxia-induci... | MARK AS OVER ANNOTATED | Summary: This paper showed that ablation of BECN1 enhances cell death under hypoxia, suggesting autophagy provides survival. However, this is through autophagy function, not direct cell death regulation. Reason: OVER-ANNOTATION. The paper states "The ablation of Beclin1, a major actor of autophagy, enhances cell death under hypoxic conditions" - this shows BECN1 promotes survival through AUTOPHAGY, not direct anti-apoptotic activity. The anti-death effect is secondary to autophagy function. Supporting Evidence: PMID:19273585 The ablation of Beclin1, a major actor of autophagy, enhances cell death under hypoxic conditions |
| GO:0032473 cytoplasmic side of mitochondrial outer membrane | IDA PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | ACCEPT | Summary: BECN1 associates with mitochondrial outer membrane, particularly MAMs. Reason: Supports mitophagy function. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0005776 autophagosome | ISS PMID:23798385 Decorin causes autophagy in endothelial cells via Peg3. | ACCEPT | Summary: BECN1 localizes to autophagosomes. Reason: Core localization. Supporting Evidence: PMID:23798385 Decorin causes autophagy in endothelial cells via Peg3. |
| GO:0006914 autophagy | IDA PMID:25891078 IRGM governs the core autophagy machinery to conduct antimic... | ACCEPT | Summary: Direct demonstration of BECN1 in autophagy through IRGM interaction study. Reason: Core function. Supporting Evidence: PMID:25891078 2015 Apr 16. IRGM governs the core autophagy machinery to conduct antimicrobial defense. |
| GO:0065003 protein-containing complex assembly | IDA PMID:25891078 IRGM governs the core autophagy machinery to conduct antimic... | ACCEPT | Summary: BECN1 assembles into PI3KC3 complexes. Reason: Core function of BECN1 as scaffold. Supporting Evidence: PMID:25891078 2015 Apr 16. IRGM governs the core autophagy machinery to conduct antimicrobial defense. |
| GO:0005515 protein binding | IPI PMID:17659302 Molecular basis of Bcl-xL's target recognition versatility r... | REMOVE | Summary: Structural study of BCL-XL in complex with BECN1 BH3 domain. Reason: Generic protein binding. The specific BCL-XL binding is relevant for autophagy regulation. Supporting Evidence: PMID:17659302 2007 Jun 30. Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of Beclin-1. |
| GO:0005515 protein binding | IPI PMID:18797192 Molecular basis of the regulation of Beclin 1-dependent auto... | REMOVE | Summary: Gamma-herpesvirus BCL-2 homolog M11 regulation of BECN1-dependent autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:18797192 Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11. |
| GO:0005515 protein binding | IPI PMID:24115198 Intrinsically disordered regions in autophagy proteins. | REMOVE | Summary: Intrinsically disordered regions in autophagy proteins including BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24115198 Intrinsically disordered regions in autophagy proteins. |
| GO:0005515 protein binding | IPI PMID:27046249 The BECN1 N-terminal domain is intrinsically disordered. | REMOVE | Summary: BECN1 N-terminal domain is intrinsically disordered. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:27046249 The BECN1 N-terminal domain is intrinsically disordered. |
| GO:0005515 protein binding | IPI PMID:30626284 Structural insights into BCL2 pro-survival protein interacti... | REMOVE | Summary: Structural study of BCL2-BECN1 interaction after STK4/MST1 phosphorylation. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:30626284 2019 Jan 9. Structural insights into BCL2 pro-survival protein interactions with the key autophagy regulator BECN1 following phosphorylation by STK4/MST1. |
| GO:0005515 protein binding | IPI PMID:30767700 Members of the autophagy class III phosphatidylinositol 3-ki... | REMOVE | Summary: PI3KC3 complex members interact with GABARAP/GABARAPL1 via LIR motifs. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:30767700 2019 Mar 4. Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. |
| GO:0010506 regulation of autophagy | IDA PMID:18797192 Molecular basis of the regulation of Beclin 1-dependent auto... | ACCEPT | Summary: Gamma-herpesvirus BCL-2 regulates BECN1-dependent autophagy. Reason: Core function. Supporting Evidence: PMID:18797192 Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11. |
| GO:0005515 protein binding | IPI PMID:22498477 The anti-apoptotic Bcl-B protein inhibits BECN1-dependent au... | REMOVE | Summary: BCL-B inhibits BECN1-dependent autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:22498477 The anti-apoptotic Bcl-B protein inhibits BECN1-dependent autophagic cell death. |
| GO:0005737 cytoplasm | IDA PMID:22498477 The anti-apoptotic Bcl-B protein inhibits BECN1-dependent au... | ACCEPT | Summary: BECN1 localized to cytoplasm. Reason: Core localization. Supporting Evidence: PMID:22498477 The anti-apoptotic Bcl-B protein inhibits BECN1-dependent autophagic cell death. |
| GO:0010508 positive regulation of autophagy | IDA PMID:21358617 Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy. | ACCEPT | Summary: Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy through BECN1. Releasing BECN1 from BCL-2 promotes autophagy. Reason: Core function. Supporting Evidence: PMID:21358617 Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy. |
| GO:0006914 autophagy | IMP PMID:28747345 ORMDL3 Facilitates the Survival of Splenic B Cells via an AT... | ACCEPT | Summary: ORMDL3 regulates autophagy through ATF6alpha-ER stress-BECN1 pathway. Reason: Core function. Supporting Evidence: PMID:28747345 2017 Jul 26. ORMDL3 Facilitates the Survival of Splenic B Cells via an ATF6Ξ±-Endoplasmic Reticulum Stress-Beclin1 Autophagy Regulatory Pathway. |
| GO:0005515 protein binding | IPI PMID:31806350 The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulat... | REMOVE | Summary: TMEM39A regulates autophagy through SAC1 trafficking affecting BECN1 complex. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:31806350 2019 Dec 2. The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1. |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Sequence similarity transfer annotation for apoptosis - problematic. Reason: OVER-ANNOTATION. BECN1 is not an apoptosis regulator. |
| GO:0005515 protein binding | IPI PMID:27031958 Nupr1/Chop signal axis is involved in mitochondrion-related ... | REMOVE | Summary: This paper studies methamphetamine-induced endothelial cell apoptosis and proposes BECN1 involvement. However, the context is non-physiological drug toxicity, and the claims about BECN1 promoting apoptosis are not well-supported. Reason: Generic protein binding. The paper's claims about BECN1 in apoptosis are questionable given known BECN1 function. Supporting Evidence: PMID:27031958 Nupr1/Chop signal axis is involved in mitochondrion-related endothelial cell apoptosis induced by methamphetamine. |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | IMP PMID:27031958 Nupr1/Chop signal axis is involved in mitochondrion-related ... | MARK AS OVER ANNOTATED | Summary: This paper claims BECN1 promotes apoptosis through Nupr1/Chop pathway in methamphetamine-exposed endothelial cells. However, this is a specific toxicological context and does not reflect core BECN1 function. The paper states BECN1 binds BCL2 and releases it for apoptosis, but this misinterprets the BECN1-BCL2 interaction which regulates autophagy. Reason: OVER-ANNOTATION. This paper misinterprets BECN1 function. BECN1 is an autophagy protein. Its interaction with BCL2 regulates autophagy, not apoptosis. The context (drug toxicity) does not reflect physiological BECN1 function. Supporting Evidence: PMID:27031958 Nupr1/Chop signal axis is involved in mitochondrion-related endothelial cell apoptosis induced by methamphetamine. |
| GO:0032465 regulation of cytokinesis | IMP PMID:20208530 PtdIns(3)P controls cytokinesis through KIF13A-mediated recr... | KEEP AS NON CORE | Summary: PI3KC3 complex generates PI3P at midbody for cytokinesis regulation. This is a non-autophagy function of BECN1. Reason: Secondary function. BECN1 in PI3KC3-C2 regulates cytokinesis through PI3P. Supporting Evidence: PMID:20208530 PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody. |
| GO:0019901 protein kinase binding | IPI PMID:27853422 ROCK1 Is Associated with Alzheimer's Disease-Specific Plaque... | ACCEPT | Summary: ROCK1 interacts with BECN1 and affects autophagosome formation. Reason: BECN1 is phosphorylated by multiple kinases that regulate its activity. Supporting Evidence: PMID:27853422 eCollection 2016. ROCK1 Is Associated with Alzheimer's Disease-Specific Plaques, as well as Enhances Autophagosome Formation But not Autophagic AΞ² Clearance. |
| GO:0005515 protein binding | IPI PMID:28479384 Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in ... | REMOVE | Summary: BECN1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:28479384 Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer cells. |
| GO:0045022 early endosome to late endosome transport | IMP PMID:26783301 Negative regulation of phosphatidylinositol 3-phosphate leve... | ACCEPT | Summary: BECN1 in PI3KC3-C2 regulates PI3P levels in endosome conversion. Reason: Related to PI3KC3-C2 endocytic trafficking function. Supporting Evidence: PMID:26783301 Negative regulation of phosphatidylinositol 3-phosphate levels in early-to-late endosome conversion. |
| GO:0051020 GTPase binding | IPI PMID:25891078 IRGM governs the core autophagy machinery to conduct antimic... | ACCEPT | Summary: IRGM is a GTPase that binds BECN1 to regulate autophagy. Reason: BECN1 interacts with small GTPases like Rab proteins and IRGM. Supporting Evidence: PMID:25891078 IRGM interacts with ULK1 and Beclin 1 and promotes their co-assembly |
| GO:0006914 autophagy | IMP PMID:23184933 XBP1 mRNA splicing triggers an autophagic response in endoth... | ACCEPT | Summary: XBP1 splicing triggers autophagy through BECN1 transcriptional activation. Reason: Core function. Supporting Evidence: PMID:23184933 2012 Nov 26. XBP1 mRNA splicing triggers an autophagic response in endothelial cells through BECLIN-1 transcriptional activation. |
| GO:0000423 mitophagy | IMP PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | ACCEPT | Summary: BECN1 membrane association and ATG14-dependent phosphorylation regulate BECN1-mediated autophagy including mitophagy. Reason: Core function. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0098780 response to mitochondrial depolarisation | IMP PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | ACCEPT | Summary: BECN1 responds to mitochondrial depolarization by localizing to mitochondria for mitophagy. Reason: Relates to mitophagy function. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0005515 protein binding | IPI PMID:22095288 PKD is a kinase of Vps34 that mediates ROS-induced autophagy... | REMOVE | Summary: PKD phosphorylates VPS34 downstream of DAPK to mediate autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:22095288 Nov 18. PKD is a kinase of Vps34 that mediates ROS-induced autophagy downstream of DAPk. |
| GO:0006914 autophagy | IDA PMID:23629966 Deacetylation of p53 induces autophagy by suppressing Bmf ex... | ACCEPT | Summary: Deacetylation of p53 induces autophagy through BECN1. Reason: Core function. Supporting Evidence: PMID:23629966 Deacetylation of p53 induces autophagy by suppressing Bmf expression. |
| GO:0005515 protein binding | IPI PMID:24113155 Placental autophagy regulation by the BOK-MCL1 rheostat. | REMOVE | Summary: BOK-MCL1 rheostat regulates placental autophagy through BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24113155 Placental autophagy regulation by the BOK-MCL1 rheostat. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6781779 | ACCEPT | Summary: USP13 deubiquitinates BECN1 in cytosol. Reason: Core localization. |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | NAS PMID:25215947 AMBRA1 is able to induce mitophagy via LC3 binding, regardle... | UNDECIDED | Summary: AMBRA1 can induce mitophagy via LC3 binding regardless of PARKIN. Connection to PI3K/AKT signaling may be indirect. Reason: Need more evidence for direct BECN1 role in PI3K/AKT signaling. Supporting Evidence: PMID:25215947 Sep 12. AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1. |
| GO:0005515 protein binding | IPI PMID:26347139 TRIM-mediated precision autophagy targets cytoplasmic regula... | REMOVE | Summary: TRIM-mediated precision autophagy targeting cytoplasmic innate immunity regulators. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:26347139 TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | ACCEPT | Summary: TRIM proteins regulate autophagy by direct recognition and can target autophagic substrates including through BECN1 interaction. Reason: BECN1 interacts with multiple E3 ligases for regulation. Supporting Evidence: PMID:25127057 2014 Aug 7. TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition. |
| GO:0005515 protein binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | REMOVE | Summary: TRIM5 interacts with BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:25127057 2014 Aug 7. TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition. |
| GO:0032465 regulation of cytokinesis | IMP PMID:20643123 A phosphatidylinositol 3-kinase class III sub-complex contai... | KEEP AS NON CORE | Summary: PI3KC3 sub-complex with VPS15, VPS34, BECN1, UVRAG, BIF-1 regulates cytokinesis. Reason: Secondary function through PI3KC3-C2. Supporting Evidence: PMID:20643123 Epub 2010 Jul 17. A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic. |
| GO:0032801 receptor catabolic process | IMP PMID:20643123 A phosphatidylinositol 3-kinase class III sub-complex contai... | ACCEPT | Summary: PI3KC3 regulates degradative endocytic traffic including receptor degradation. Reason: PI3KC3-C2 function in receptor trafficking. Supporting Evidence: PMID:20643123 Epub 2010 Jul 17. A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672012 | ACCEPT | Summary: Beclin-1 complex phosphorylates PtdIns in cytosol. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5679205 | ACCEPT | Summary: ULK1 phosphorylates Beclin-1 in cytosol. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5682385 | ACCEPT | Summary: Phagophore extends from PI3P-enriched structure. Reason: Core localization. |
| GO:0005739 mitochondrion | IMP PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | ACCEPT | Summary: BECN1 localizes to mitochondria for mitophagy function. Reason: Supports mitophagy function. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0000045 autophagosome assembly | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence similarity annotation - consistent with core function. Reason: Core function. |
| GO:0016236 macroautophagy | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence similarity annotation - consistent with core function. Reason: Core function. |
| GO:0035032 phosphatidylinositol 3-kinase complex, class III | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence similarity annotation - BECN1 is obligate component of PI3KC3. Reason: Core localization. |
| GO:0042149 cellular response to glucose starvation | ISS GO_REF:0000024 | ACCEPT | Summary: Autophagy is induced by glucose starvation. Reason: Core function - metabolic stress triggers autophagy. |
| GO:0005515 protein binding | IPI PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | REMOVE | Summary: Membrane association and ATG14-dependent phosphorylation of BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0005768 endosome | IDA PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | ACCEPT | Summary: BECN1 localizes to endosomes. Reason: Related to PI3KC3-C2 function. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0005783 endoplasmic reticulum | IDA PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | ACCEPT | Summary: BECN1 localizes to ER, particularly for autophagosome nucleation. Reason: Core localization for autophagy initiation. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0043548 phosphatidylinositol 3-kinase binding | IPI PMID:23878393 Role of membrane association and Atg14-dependent phosphoryla... | ACCEPT | Summary: BECN1 directly binds VPS34 (PI3KC3). Reason: Core molecular function. Supporting Evidence: PMID:23878393 Jul 22. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. |
| GO:0005515 protein binding | IPI PMID:24056301 The deubiquitylase USP33 discriminates between RALB function... | REMOVE | Summary: USP33 deubiquitylase discriminates RALB functions in autophagy. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:24056301 The deubiquitylase USP33 discriminates between RALB functions in autophagy and innate immune response. |
| GO:0005515 protein binding | IPI PMID:23182941 A novel ER-localized transmembrane protein, EMC6, interacts ... | REMOVE | Summary: EMC6 interacts with RAB5A and regulates autophagy through BECN1. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:23182941 A novel ER-localized transmembrane protein, EMC6, interacts with RAB5A and regulates cell autophagy. |
| GO:0006914 autophagy | IMP PMID:24056303 PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and A... | ACCEPT | Summary: UVRAG coordinates Golgi-ER retrograde transport with BECN1 complex. Reason: Core function. Supporting Evidence: PMID:24056303 PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex. |
| GO:0007080 mitotic metaphase chromosome alignment | IMP PMID:23478334 Beclin-1 is required for chromosome congression and proper o... | KEEP AS NON CORE | Summary: BECN1 is required for proper chromosome congression and kinetochore assembly. Non-autophagy function. Reason: Secondary/non-autophagy function. Supporting Evidence: PMID:23478334 Beclin-1 is required for chromosome congression and proper outer kinetochore assembly. |
| GO:1902425 positive regulation of attachment of mitotic spindle microtubules to kinetochore | IMP PMID:23478334 Beclin-1 is required for chromosome congression and proper o... | KEEP AS NON CORE | Summary: BECN1 affects kinetochore-microtubule attachment. Non-autophagy function. Reason: Secondary/non-autophagy function. Supporting Evidence: PMID:23478334 Beclin-1 is required for chromosome congression and proper outer kinetochore assembly. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1169406 | ACCEPT | Summary: ISGylation of host proteins in cytosol. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1632857 | ACCEPT | Summary: ULK1 phosphorylates AMBRA1:BECN1 complex. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1678841 | ACCEPT | Summary: ISG15 deconjugating enzyme USP18 regulation. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5678313 | ACCEPT | Summary: AMBRA1:DYNLL binds BECN1 complex. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5678315 | ACCEPT | Summary: BECN1 complex dissociates from DYNLL. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5679266 | ACCEPT | Summary: Beclin-1 complex translocates to ER. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9755359 | ACCEPT | Summary: SARS-CoV-2 ORF8:class I MHC binds BECN1. Reason: Core localization. |
| GO:0005515 protein binding | IPI PMID:17724469 Reduced expression of vacuole membrane protein 1 affects the... | REMOVE | Summary: VMP1 affects invasion capacity through BECN1 interaction. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:17724469 Reduced expression of vacuole membrane protein 1 affects the invasion capacity of tumor cells. |
| GO:0005515 protein binding | IPI PMID:19270696 Two Beclin 1-binding proteins, Atg14L and Rubicon, reciproca... | REMOVE | Summary: ATG14L and Rubicon reciprocally regulate autophagy through BECN1 binding. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:19270696 Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. |
| GO:0005515 protein binding | IPI PMID:21962518 Beclin1 controls the levels of p53 by regulating the deubiqu... | REMOVE | Summary: BECN1 controls p53 levels through USP10/USP13 deubiquitination activity. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:21962518 Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13. |
| GO:0005515 protein binding | IPI PMID:16417406 Hem-1 complexes are essential for Rac activation, actin poly... | REMOVE | Summary: Hem-1 complexes study - BECN1 interaction in neutrophil chemotaxis. Reason: Generic protein binding term is uninformative. Supporting Evidence: PMID:16417406 Hem-1 complexes are essential for Rac activation, actin polymerization, and myosin regulation during neutrophil chemotaxis. |
| GO:0006968 cellular defense response | TAS PMID:9765397 Protection against fatal Sindbis virus encephalitis by becli... | ACCEPT | Summary: Original paper discovering BECN1 showing it protects against viral encephalitis. Reason: BECN1 participates in xenophagy/antiviral autophagy. Supporting Evidence: PMID:9765397 These findings demonstrate that Beclin is a novel Bcl-2-interacting cellular protein that may play a role in antiviral host defense. |
| GO:0043066 negative regulation of apoptotic process | TAS PMID:9765397 Protection against fatal Sindbis virus encephalitis by becli... | MARK AS OVER ANNOTATED | Summary: The original BECN1 paper showed it protected against virus-induced neuronal death. However, this was likely through autophagy-mediated viral clearance, not direct anti-apoptotic activity. The paper focused on BECN1's BCL2 interaction but the functional significance was later shown to be autophagy regulation. Reason: OVER-ANNOTATION. The original paper interpreted BECN1 as anti-apoptotic due to BCL2 interaction. Later work established that this interaction regulates autophagy, and the protective effect is through autophagy-mediated viral clearance, not direct anti-apoptotic activity. Supporting Evidence: PMID:9765397 These findings demonstrate that Beclin is a novel Bcl-2-interacting cellular protein that may play a role in antiviral host defense. |
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Download this section (compressed HTML)Q: What is the precise mechanism by which BECN1 membrane association regulates autophagosome size versus number? The PMID:23878393 study identified a membrane-association domain but the molecular mechanism remains unclear.
Q: Are there isoform-specific or cell type-specific differences in BECN1 function between autophagy and endocytic trafficking? BECN1 participates in both PI3KC3-C1 (autophagy) and PI3KC3-C2 (trafficking) but the determinants of which complex forms are not fully understood.
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