HER-2
Overview[edit | edit source]
H2AFX is a gene that encodes a member of the histone H2A family, which is a component of the histone octamer in the nucleosome core. The H2AFX protein plays a crucial role in the cellular response to DNA damage and is involved in the maintenance of genomic stability.
Structure[edit | edit source]
The H2AFX gene is located on chromosome 11 in humans and is composed of several exons. The protein product, H2A.X, is a variant of the histone H2A and is characterized by a unique C-terminal tail that contains a serine residue at position 139. This serine residue is a critical site for phosphorylation in response to DNA double-strand breaks.
Function[edit | edit source]
H2AFX is primarily involved in the DNA damage response. Upon the occurrence of DNA double-strand breaks, the serine 139 residue of H2A.X is rapidly phosphorylated by the ATM, ATR, and DNA-PK kinases. This phosphorylated form of H2A.X is known as γ-H2A.X and serves as a marker for DNA damage.
The formation of γ-H2A.X foci at sites of DNA damage facilitates the recruitment of DNA repair proteins, including BRCA1, MDC1, and 53BP1. These proteins are essential for the repair of DNA double-strand breaks through homologous recombination and non-homologous end joining pathways.
Clinical Significance[edit | edit source]
Mutations or alterations in the expression of H2AFX can lead to genomic instability and have been associated with various cancers. The presence of γ-H2A.X is often used as a biomarker for DNA damage in cancer cells and can be indicative of the effectiveness of cancer therapies that induce DNA damage.
Research Applications[edit | edit source]
H2AFX and its phosphorylated form, γ-H2A.X, are widely used in research to study the mechanisms of DNA repair and the cellular response to DNA damage. The detection of γ-H2A.X foci is a common method for assessing DNA damage in cells exposed to ionizing radiation or chemotherapeutic agents.
Also see[edit | edit source]
References[edit | edit source]
| Excision repair | |
|---|---|
| Other forms of repair | |
| Other/ungrouped proteins | |
| Regulation | |
| Other/ungrouped | |
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