Tag: DNA damage response

Post-translational modifications are essential regulators of cell-cycle progression. Learn how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and other PTMs control CDKs, cyclins, checkpoints, DNA replication, mitosis, and protein degradation.

Protein ubiquitination is a fundamental post-translational modification that regulates protein degradation, cellular signaling, DNA repair, autophagy, protein trafficking and cellular homeostasis.

Protein ADP-ribosylation is an important post-translational modification that uses NAD+ to regulate proteins and cellular pathways. Explore mono- and poly-ADP-ribosylation, PARP enzymes, DNA repair, chromatin regulation, cancer, metabolism, inflammation, and cell death.

The DNA damage response is a cellular defense system that detects DNA damage, coordinates repair, regulates cell-cycle checkpoints, and protects the stability of the genome.

ATM is a key protein kinase in the DNA damage response. Discover how it detects DNA double-strand breaks, activates signaling pathways, regulates the cell cycle, and helps maintain genome stability.

ATR is a key protein kinase that protects cells from replication stress and DNA damage. Explore how ATR detects single-stranded DNA, stabilizes replication forks, activates CHK1, and maintains genome stability.

ATM, ATR, DNA-PK, and p53 are key regulators of the DNA damage response. Learn how these pathways detect DNA damage, coordinate repair, control the cell cycle, and protect genome stability.

DNA-PK is a key component of the DNA damage response that helps repair DNA double-strand breaks through the non-homologous end joining pathway and supports genome stability.

K63‑linked ubiquitination is a non‑degradative signalling modification that assembles scaffold‑like ubiquitin chains regulating DNA repair, NF‑κB activation, receptor endocytosis and autophagy. Built by UBE2N/UBE2V1 and specialised E3 ligases, K63 chains coordinate dynamic cellular responses without targeting proteins for proteasomal degradation.

Mdm2 is a RING‑type E3 ubiquitin ligase that controls p53 stability through ubiquitination, nuclear export and proteasomal degradation. By interacting with p53, Mdmx/Mdm4 and ARF, Mdm2 regulates DNA‑damage responses, cell‑cycle progression and oncogenesis, making it a central determinant of tumour development and genome stability.

HECT ubiquitin ligases are catalytic E3 enzymes that form a thioester intermediate with ubiquitin, allowing precise control of ubiquitin‑chain architecture. Through NEDD4‑family ligases, HERC proteins and HUWE1, the HECT class regulates receptor endocytosis, DNA‑damage signalling, proteostasis and diverse cellular stress responses.

K48‑linked ubiquitination is the principal degradation signal in eukaryotic cells, directing proteins to the 26S proteasome. Built by E1, E2 and E3 enzymes, K48‑linked chains regulate protein turnover, cell‑cycle progression and DNA‑damage responses, forming a central mechanism for maintaining proteostasis and preventing toxic protein accumulation.

SYCP2 is a meiosis‑specific protein that forms the lateral elements of the synaptonemal complex. Its interaction with SYCP3 is essential for chromosome pairing, recombination, and fertility.

SYCP1 is a meiosis‑specific protein that forms the transverse filaments of the synaptonemal complex. Its correct assembly is essential for homologous chromosome pairing, recombination, and fertility.

SYCP3 is a meiosis‑specific protein essential for chromosomal synapsis and the formation of the synaptonemal complex. Mutations in SYCP3 are linked to meiotic arrest, infertility, and genomic instability.