Protein lysine acetylation in cellular function and its role in cancer manifestation.
Lysine acetylation appears to be crucial for diverse biological phenomena, including all the DNA-templated processes, metabolism, cytoskeleton dynamics, cell signaling, and circadian rhythm. A growing number of cellular proteins have now been identified to be acetylated and constitute the complex cellular acetylome. Cross-talk among protein acetylation together with other post-translational modifications fine-tune the cellular functions of different protein machineries. Dysfunction of acetylation process is often associated with several diseases, especially cancer. This review focuses on the recent advances in the role of protein lysine acetylation in diverse cellular functions and its implications in cancer manifestation.
Arif
Mohammed
M
Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur (P.O.), Bangalore-560 064, Karnataka, India.
Senapati
Parijat
P
Shandilya
Jayasha
J
Kundu
Tapas K
TK
D000107:Acetylation; D051046:Amino-Acid N-Acetyltransferase / Q000378:metabolism; D000818:Animals; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D009363:Neoplasm Proteins; D051046:Amino-Acid N-Acetyltransferase; D008239:Lysine