Journal
JOURNAL OF CELLULAR PHYSIOLOGY
Volume 227, Issue 8, Pages 3027-3035Publisher
WILEY-BLACKWELL
DOI: 10.1002/jcp.23044
Keywords
-
Categories
Funding
- National Research Foundation of Korea (NRF)
- inistry of Education, Science, and Technology of Korea [NRF-2009-0072774, KRF-2008-359-C00026]
- National Research Foundation of Korea [2008-359-C00026] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ask authors/readers for more resources
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: 30273035, 2012. (c) 2011 Wiley Periodicals, Inc.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available