Bcl-2-like protein 1
Bcl-2-like protein 1
Bcl-2-like protein 1, also known as BCL2L1, is a protein that in humans is encoded by the BCL2L1 gene. It is a member of the Bcl-2 protein family, which plays a crucial role in regulating apoptosis, or programmed cell death. Bcl-2-like protein 1 is involved in the control of cell survival and is known to inhibit apoptosis.
Structure[edit | edit source]
Bcl-2-like protein 1 is composed of four Bcl-2 homology (BH) domains, namely BH1, BH2, BH3, and BH4. These domains are essential for its anti-apoptotic function. The BH3 domain, in particular, is critical for interactions with pro-apoptotic proteins.
Function[edit | edit source]
The primary function of Bcl-2-like protein 1 is to prevent apoptosis by inhibiting the release of cytochrome c from mitochondria, which is a key step in the apoptotic pathway. It also regulates mitochondrial membrane permeability and plays a role in maintaining mitochondrial integrity.
Role in Cancer[edit | edit source]
Dysregulation of Bcl-2-like protein 1 has been implicated in various cancers. Overexpression of Bcl-2-like protein 1 can promote cell survival and contribute to tumor growth by preventing apoptosis. Targeting Bcl-2-like protein 1 has emerged as a potential therapeutic strategy for cancer treatment.
Interactions[edit | edit source]
Bcl-2-like protein 1 interacts with a variety of proteins involved in the apoptotic pathway, including pro-apoptotic members of the Bcl-2 family such as Bax and Bak. These interactions determine the balance between cell survival and cell death.
Clinical Significance[edit | edit source]
Due to its role in apoptosis regulation, Bcl-2-like protein 1 has been studied as a potential target for drug development in cancer therapy. Inhibitors of Bcl-2-like protein 1 are being investigated for their ability to induce apoptosis in cancer cells selectively.
See also[edit | edit source]
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