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| | ==Structure of Beclin1-UVRAG coiled coil domain complex== | | ==Structure of Beclin1-UVRAG coiled coil domain complex== |
| - | <StructureSection load='5yr0' size='340' side='right' caption='[[5yr0]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='5yr0' size='340' side='right'caption='[[5yr0]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yr0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YR0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yr0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YR0 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yr0 OCA], [http://pdbe.org/5yr0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yr0 RCSB], [http://www.ebi.ac.uk/pdbsum/5yr0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yr0 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yr0 OCA], [https://pdbe.org/5yr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yr0 RCSB], [https://www.ebi.ac.uk/pdbsum/5yr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yr0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BECN1_MOUSE BECN1_MOUSE]] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense.<ref>PMID:10604474</ref> <ref>PMID:12372286</ref> <ref>PMID:19270693</ref> [[http://www.uniprot.org/uniprot/UVRAG_MOUSE UVRAG_MOUSE]] Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P). During autophagy acts as regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3. Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2. Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events. Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion. In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly (By similarity).[UniProtKB:Q9P2Y5] Involved in maintaining chromosomal stability. Promotes DNA double-strand break (DSB) repair by association with DNA-dependent protein kinase complex DNA-PK and activating it in non-homologous end joining (NHEJ). Required for centrosome stability and proper chromosome segregation (By similarity).[UniProtKB:Q9P2Y5] | + | [https://www.uniprot.org/uniprot/BECN1_MOUSE BECN1_MOUSE] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense.<ref>PMID:10604474</ref> <ref>PMID:12372286</ref> <ref>PMID:19270693</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: He, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Pan, X]] | + | [[Category: Mus musculus]] |
| - | [[Category: Zhao, Y]] | + | [[Category: He Y]] |
| - | [[Category: Autophagy regulator]] | + | [[Category: Pan X]] |
| - | [[Category: Endocytosis]] | + | [[Category: Zhao Y]] |
| Structural highlights
Function
BECN1_MOUSE Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense.[1] [2] [3]
References
- ↑ Liang XH, Jackson S, Seaman M, Brown K, Kempkes B, Hibshoosh H, Levine B. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature. 1999 Dec 9;402(6762):672-6. PMID:10604474 doi:http://dx.doi.org/10.1038/45257
- ↑ Yue Z, Horton A, Bravin M, DeJager PL, Selimi F, Heintz N. A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice. Neuron. 2002 Aug 29;35(5):921-33. PMID:12372286
- ↑ Zhong Y, Wang QJ, Li X, Yan Y, Backer JM, Chait BT, Heintz N, Yue Z. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat Cell Biol. 2009 Apr;11(4):468-76. doi: 10.1038/ncb1854. Epub 2009 Mar 8. PMID:19270693 doi:http://dx.doi.org/10.1038/ncb1854
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