Mitofusin 2 but not mitofusin 1 mediates Bcl-XL-induced mitochondrial aggregation
MFN1
MFN2
Bcl-2 Family
DOI:
10.1242/jcs.245001
Publication Date:
2020-09-21T16:12:23Z
AUTHORS (10)
ABSTRACT
Bcl-2 family proteins, as central players of the apoptotic program, participate in regulation mitochondrial network. Here, a quantitative live-cell fluorescence resonance energy transfer (FRET) two-hybrid assay was used to confirm homo-/hetero-oligomerization mitofusins 2 and 1 (MFN2 MFN1), also demonstrate binding MFN2 MFN1 with 1:1 stoichiometry. A FRET for living cells co-expressing CFP-labeled Bcl-XL (an anti-apoptotic protein encoded by BCL2L1) YFP-labeled or demonstrated Neither nor bound monomeric Bax healthy cells, but both bind punctate (pro-apoptotic protein) during apoptosis. Oligomerized Bak (also known BAK1; pro-apoptotic only associated not MFN2. Moreover, co-expression had same effect expression alone staurosporine-induced apoptosis, indicating has its full ability when complexed MFN1. However, knockdown reduced aggregation induced overexpression Bcl-XL, that mediates Bcl-XL-induced aggregation.
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