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PERSPECTIVE
1 Center for Advanced Biotechnology and Medicine, 2 Howard Hughes Medical Institute, Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA; 3 Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, USA; 4 Cancer Institute of New Jersey, New Brunswick, New Jersey 08901, USA
| The first 100 words of the full text of this article appear below. |
The BCL-2 family of proteins regulates apoptosis, and proper control of this process is required for normal development and for preventing disease (Adams 2003
; Danial and Korsmeyer 2004). After years of identifying components and deciphering the regulatory pathways that control apoptosis, we are now at the point of exploiting this knowledge in sophisticated ways for therapeutic intervention in disease conditions such as cancer. Members of the BCL-2 family fall into three different classes of proteins based on conservation of BCL-2 homology (BH1-4) domains: multidomain anti-apoptotic proteins (BCL-2, BCL-xL, MCL-1, BCL-w, and BFL-1/A1), multidomain proapoptotic proteins (BAX and
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It's all about protein conformation |
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Who's got your BAK? |
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MCL-1 keeps BAK on a leash |
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Who's doing what to whom? |
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BH3-only proteins reveal their specificity |
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NOXA targets MCL-1, unleashing BAK |
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BCL-xL picks up the slack and has your BAK |
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Consequences for therapeutic modulation of apoptosis |
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Looking upstream of BAK |
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Details are important |
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