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Endoplasmic reticulum‐specific BH3‐only protein BNIP1 induces mitochondrial fragmentation in a Bcl‐2‐ and Drp1‐dependent manner
Author(s) -
Ryu SeungWook,
Choi Kyungsun,
Yoon Jonghee,
Kim Sunchang,
Choi Chulhee
Publication year - 2012
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.23044
Subject(s) - mitochondrial fission , endoplasmic reticulum , microbiology and biotechnology , mitochondrion , fragmentation (computing) , dnm1l , mitochondrial apoptosis induced channel , dnaja3 , biology , apoptosis , mitochondrial fusion , chemistry , mitochondrial dna , inner mitochondrial membrane , biochemistry , gene , ecology
Bcl‐2/adenovirus E1B 19‐kDa interacting protein 1 (BNIP1), which is predominantly localized to the endoplasmic reticulum (ER), is a pro‐apoptotic Bcl‐2 homology domain 3 (BH3)‐only protein. Here, we show that the expression of BNIP1 induced not only a highly interconnected ER network but also mitochondrial fragmentation in a BH3 domain‐dependent manner. Functional analysis demonstrated that BNIP1 expression increased dynamin‐related protein 1 (Drp1) expression followed by the mitochondrial translocation of Drp1 and subsequent mitochondrial fission. Both BNIP1‐induced mitochondrial fission and the translocation of Drp1 were abrogated by Bcl‐2 overexpression. These results collectively indicate that ER‐specific BNIP1 plays an important role in mitochondrial dynamics by modulating the mitochondrial fission protein Drp1 in a BH3 domain‐dependent fashion. J. Cell. Physiol. 227: 3027–3035, 2012. © 2011 Wiley Periodicals, Inc.