BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis

The execution phase of apoptosis is characterized by marked changes in cell morphology that include contraction and membrane blebbing. Little is known about the mechanisms underlying this process. We report here the identification of a novel member of BNIPL family, designated Bcl-2/adenovirus E1B 19...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2003-08, Vol.308 (2), p.379-385
Main Authors: Qin, Wenxin, Hu, Jian, Guo, Minglei, Xu, Jian, Li, Jinjun, Yao, Genfu, Zhou, Xiaomei, Jiang, Huiqiu, Zhang, Pingping, Shen, Li, Wan, Dafang, Gu, Jianren
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing
Apoptosis
Apoptosis - physiology
Base Sequence
BCH domain
BNIPL
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
cdc42 GTP-Binding Protein - metabolism
Direct yeast two-hybrid
DNA, Complementary - genetics
High-throughput transfection
Humans
In Vitro Techniques
Molecular Sequence Data
Protein Binding
Protein Structure, Tertiary
Proto-Oncogene Proteins c-bcl-2 - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Deletion
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Summary:The execution phase of apoptosis is characterized by marked changes in cell morphology that include contraction and membrane blebbing. Little is known about the mechanisms underlying this process. We report here the identification of a novel member of BNIPL family, designated Bcl-2/adenovirus E1B 19 kDa interacting protein 2 like-2 (BNIPL-2), which interacts with Bcl-2 and Cdc42GAP. We found that the human BNIPL-2 shares homology to human BNIP-2 and also possesses a BNIP-2 and Cdc42GAP homology (BCH) domain. Deletion experiments indicated that the BCH domain of BNIPL-2 is critical for its interactions with the Bcl-2 and Cdc42GAP and also for its cell death-inducing function. Our data showed that BNIPL-2 may be a linker protein located at the front end of Bcl-2 pathway for DNA fragmentation and Cdc42 signaling for morphological changes during apoptosis. We propose that BNIPL-2 protein may play an important role in regulation of both pathways for DNA fragmentation and for formation of membrane blebs in apoptotic cells.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(03)01387-1