DELE1: A Potential Drug Target and Biomarker for Cell Death Enhancer 1 in Cancer

Target Name: DELE1

NCBI ID: G9812

DELE1: A Potential Drug Target and Biomarker for Cell Death Enhancer 1 in Cancer

Abstract:

DELE1 (DAP3-binding cell death enhancer 1) is a non-coding RNA that has been identified as a potential drug target and biomarker for cancer. Its expression has been observed in various types of cancer, including breast, ovarian, and colorectal cancer. DELE1 has been shown to promote cell death by activating the DAP3 protein, which is a key regulator of cell survival.

In this article, we will review the current research on DELE1 and its potential as a drug target and biomarker for cancer. We will discuss the structure and function of DELE1, and its potential interactions with other molecules. We will also examine the potential clinical applications of DELE1 as a drug target and biomarker, and discuss the challenges and opportunities in its development as a new cancer therapeutic.

Structure and Function:

DELE1 is a non-coding RNA that was identified as a potential drug target and biomarker for cancer. It is composed of 199 base pairs of RNA and has a calculated molecular weight of 19.8 kDa. DELE1 is expressed in various tissues and organs, including brain , heart, liver, and cancer cells.

The DELE1 protein is composed of two distinct domains: a N-terminal domain and a C-terminal domain. The N-terminal domain consists of a single alpha-helix and a long flexible region that is involved in protein-protein interactions. The C -terminal domain is a fusiform domain that is responsible for the binding of DELE1 to its protein partner, DAP3.

DELE1 has been shown to promote cell death by activating the DAP3 protein. DAP3 is a protein that plays a critical role in regulating cell survival by controlling the levels of mitochondrial ATP. DAP3 has been shown to promote cell survival by inhibiting the intrinsic cell death signaling pathway, which is a pathway that promotes cell death when oxygen and nutrients are depleted.

In cancer cells, DAP3 has been shown to be overexpressed, which may contribute to the development and progression of cancer. By inhibiting the DAP3 protein, DELE1 has been shown to induce cell death in cancer cells. This is consistent with the idea that DELE1 may be a potential drug target for cancer.

Potential Clinical Applications:

The potential clinical applications of DELE1 as a drug target and biomarker for cancer are significant. DELE1 has been shown to be overexpressed in various types of cancer, including breast, ovarian, and colorectal cancer. This suggests that DELE1 may be a useful target for cancer therapies that are designed to inhibit the growth and survival of cancer cells.

One potential approach to using DELE1 as a drug target is to inhibit its expression by small molecules or antibodies that target the DELE1 protein. This could be done by targeting the N-terminal or C-terminal domain of DELE1, or by targeting DAP3 itself.

Another potential approach to using DELE1 as a biomarker is to use it as a diagnostic tool for cancer. The expression of DELE1 has been shown to be overexpressed in various types of cancer, including breast, ovarian, and colorectal cancer. This suggests that DELE1 may be a useful biomarker for these cancers.

Challenges and Opportunities:

The development of DELE1 as a drug target and biomarker for cancer faces several challenges. One of the challenges is the lack of understanding of the underlying molecular mechanisms that regulate DELE1 expression. In order to fully understand the mechanisms that regulate DELE1, more research is needed to identify the specific

Protein Name: DAP3 Binding Cell Death Enhancer 1

Functions: Key activator of the integrated stress response (ISR) following mitochondrial stress (PubMed:32132706, PubMed:32132707). In response to mitochondrial stress, cleaved by the protease OMA1, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR (PubMed:32132706, PubMed:32132707). Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation (PubMed:20563667)

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