DCTN1

From WikiMD's Wellness Encyclopedia


Death-associated protein kinase 3 (DAPK3), also known as ZIPK (ZIP kinase), is a serine/threonine kinase that plays a crucial role in apoptosis, autophagy, and cell cycle regulation. DAPK3 is a member of the death-associated protein kinase family, which is involved in various cellular processes related to cell death and survival.

Structure[edit | edit source]

DAPK3 is a 454 amino acid protein with a molecular weight of approximately 51 kDa. It contains a kinase domain at the N-terminus, which is responsible for its catalytic activity. The C-terminal region of DAPK3 includes a leucine zipper motif, which is important for its dimerization and interaction with other proteins.

Function[edit | edit source]

DAPK3 is involved in the regulation of several cellular processes:

  • Apoptosis: DAPK3 is known to phosphorylate and activate various substrates that promote apoptotic cell death. It is involved in the intrinsic and extrinsic pathways of apoptosis.
  • Autophagy: DAPK3 has been implicated in the regulation of autophagy, a process that degrades and recycles cellular components. It modulates autophagic flux by interacting with key autophagy-related proteins.
  • Cell Cycle Regulation: DAPK3 plays a role in cell cycle progression, particularly in the G2/M transition. It phosphorylates and regulates proteins involved in mitosis.

Clinical Significance[edit | edit source]

Alterations in DAPK3 expression and activity have been associated with various diseases, including cancer. Overexpression or hyperactivation of DAPK3 has been observed in certain types of cancer, where it may contribute to tumor progression and resistance to apoptosis. Conversely, loss of DAPK3 function can lead to impaired cell death and increased survival of cancer cells.

Research and Therapeutic Potential[edit | edit source]

Due to its role in apoptosis and cell cycle regulation, DAPK3 is a potential target for cancer therapy. Inhibitors of DAPK3 are being investigated for their ability to sensitize cancer cells to apoptosis and enhance the efficacy of existing treatments.

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Contributors: Prab R. Tumpati, MD