Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis

Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is required both for binding to prosurvival Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors b...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 2001-09, Vol.293 (5536), p.1829-1832
Hauptverfasser: Puthalakath, Hamsa, Villunger, Andreas, O'Reilly, Lorraine A., Beaumont, Jennifer G., Coultas, Leigh, Cheney, Richard E., David C. S. Huang, Strasser, Andreas
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container_end_page 1832
container_issue 5536
container_start_page 1829
container_title Science (American Association for the Advancement of Science)
container_volume 293
creator Puthalakath, Hamsa
Villunger, Andreas
O'Reilly, Lorraine A.
Beaumont, Jennifer G.
Coultas, Leigh
Cheney, Richard E.
David C. S. Huang
Strasser, Andreas
description Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is required both for binding to prosurvival Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors by association with dynein light chain 2. Certain damage signals, such as loss of cell attachment (anoikis), unleash Bmf, allowing it to translocate and bind prosurvival Bcl-2 proteins. Thus, at least two mammalian BH3-only proteins, Bmf and Bim, function to sense intracellular damage by their localization to distinct cytoskeletal structures.
doi_str_mv 10.1126/science.1062257
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S. Huang</creatorcontrib><creatorcontrib>Strasser, Andreas</creatorcontrib><title>Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is required both for binding to prosurvival Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors by association with dynein light chain 2. Certain damage signals, such as loss of cell attachment (anoikis), unleash Bmf, allowing it to translocate and bind prosurvival Bcl-2 proteins. 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identifier ISSN: 0036-8075
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subjects Adaptor Proteins, Signal Transducing
Ageing, cell death
Amino Acid Sequence
Analysis
Animals
Anoikis
Antibodies
Apoptosis
Apoptosis Regulatory Proteins
Bcl-2-Like Protein 11
Biological and medical sciences
Calmodulin-Binding Proteins - metabolism
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
CDNA libraries
Cell Line
Cell lines
Cell physiology
Cells
Cellular biology
Cellulose nitrate
Cytoskeleton - metabolism
Developmental Stages
Drosophila Proteins
Dyneins
Family (Sociological Unit)
Family members
Fundamental and applied biological sciences. Psychology
Gene Expression Profiling
Genetic aspects
Genetic research
HEK293 cells
Humans
Libraries
Membrane Proteins
Messenger RNA
Mice
Molecular and cellular biology
Molecular Motor Proteins - metabolism
Molecular Sequence Data
Mutation
Myeloid Cell Leukemia Sequence 1 Protein
Myosin Type V
Neoplasm Proteins - genetics
Neoplasm Proteins - metabolism
Nerve Tissue Proteins - metabolism
Protein Binding
Protein Structure, Tertiary
Protein Transport
Proteins
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-bcl-2 - chemistry
Proto-Oncogene Proteins c-bcl-2 - genetics
Proto-Oncogene Proteins c-bcl-2 - metabolism
RNA, Messenger - analysis
RNA, Messenger - genetics
Spleen cells
Stimuli
T lymphocytes
Transfection
Two-Hybrid System Techniques
title Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis
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