Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/16415
DC Field | Value | Language |
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dc.contributor | Department of Applied Biology and Chemical Technology | - |
dc.creator | Li, X | - |
dc.creator | He, L | - |
dc.creator | Che, KH | - |
dc.creator | Funderburk, SF | - |
dc.creator | Pan, L | - |
dc.creator | Pan, N | - |
dc.creator | Zhang, M | - |
dc.creator | Yue, Z | - |
dc.creator | Zhao, Y | - |
dc.date.accessioned | 2015-06-23T09:09:21Z | - |
dc.date.available | 2015-06-23T09:09:21Z | - |
dc.identifier.uri | http://hdl.handle.net/10397/16415 | - |
dc.language.iso | en | en_US |
dc.publisher | Nature Publishing Group | en_US |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ | en_US |
dc.rights | © 2012 Macmillan Publishers Limited. All rights reserved. | en_US |
dc.rights | © 2012 Macmillan Publishers Limited. All rights reserved. | en_US |
dc.rights | The following publication Li, X., He, L., Che, K. et al. Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG. Nat Commun 3, 662 (2012) is available at https://dx.doi.org/10.1038/ncomms1648 | en_US |
dc.title | Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.volume | 3 | - |
dc.identifier.doi | 10.1038/ncomms1648 | - |
dcterms.abstract | Beclin 1 is a core component of the Class III Phosphatidylinositol 3-Kinase VPS34 complex. The coiled coil domain of Beclin 1 serves as an interaction platform for assembly of distinct Atg14L-and UVRAG-containing complexes to modulate VPS34 activity. Here we report the crystal structure of the coiled coil domain that forms an antiparallel dimer and is rendered metastable by a series of 'imperfect' a-d' pairings at its coiled coil interface. Atg14L and UVRAG promote the transition of metastable homodimeric Beclin 1 to heterodimeric Beclin1-Atg14L/UVRAG assembly. Beclin 1 mutants with their 'imperfect' a-d' pairings modified to enhance self-interaction, show distinctively altered interactions with Atg14L or UVRAG. These results suggest that specific utilization of the dimer interface and modulation of the homodimer-heterodimer transition by Beclin 1-interacting partners may underlie the molecular mechanism that controls the formation of various Beclin1-VPS34 subcomplexes to exert their effect on an array of VPS34-related activities, including autophagy. | - |
dcterms.accessRights | open access | en_US |
dcterms.bibliographicCitation | Nature Communications, 7 2012, v. 3, no. , p. 1-11 | - |
dcterms.isPartOf | Nature Communications | - |
dcterms.issued | 2012 | - |
dc.identifier.isi | WOS:000302060100003 | - |
dc.identifier.scopus | 2-s2.0-84862023791 | - |
dc.identifier.pmid | 22314358 | - |
dc.identifier.eissn | 2041-1723 | - |
dc.identifier.rosgroupid | r58606 | - |
dc.description.ros | 2011-2012 > Academic research: refereed > Publication in refereed journal | - |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_IR/PIRA | en_US |
dc.description.pubStatus | Published | en_US |
Appears in Collections: | Journal/Magazine Article |
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File | Description | Size | Format | |
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Li_Imperfect_Interface_Beclin1.pdf | 2.07 MB | Adobe PDF | View/Open |
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