DUSP13

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DUSP13[edit | edit source]

The DUSP13 gene

DUSP13 (Dual Specificity Phosphatase 13) is a protein-coding gene that is part of the larger family of dual-specificity phosphatases. It is located on chromosome 1 in humans and is conserved across various species, including mice and rats. DUSP13 plays a crucial role in regulating cellular signaling pathways by dephosphorylating both tyrosine and serine/threonine residues on target proteins.

Gene Structure[edit | edit source]

The DUSP13 gene spans approximately 20 kilobases and consists of 9 exons. It encodes a protein of 365 amino acids, with a predicted molecular weight of around 40 kilodaltons. The gene is transcribed into a messenger RNA (mRNA) molecule, which is then translated into the DUSP13 protein.

Function[edit | edit source]

DUSP13 acts as a phosphatase, specifically targeting phosphorylated tyrosine and serine/threonine residues on proteins. By removing phosphate groups from these residues, DUSP13 regulates the activity of various signaling pathways, including those involved in cell growth, differentiation, and survival.

Role in Cellular Signaling[edit | edit source]

DUSP13 is known to interact with several key signaling molecules, including members of the mitogen-activated protein kinase (MAPK) family. It has been shown to dephosphorylate and inactivate MAPKs such as ERK1/2, JNK, and p38, thereby modulating their downstream signaling cascades. This regulation is crucial for maintaining cellular homeostasis and preventing aberrant signaling events.

Clinical Significance[edit | edit source]

Research has implicated DUSP13 in various diseases and conditions. For example, dysregulation of DUSP13 expression or activity has been observed in certain types of cancer, including breast cancer and colorectal cancer. Additionally, DUSP13 has been linked to neurodegenerative disorders, such as Alzheimer's disease, where abnormal signaling pathways play a role in disease progression.

References[edit | edit source]


See Also[edit | edit source]

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Contributors: Prab R. Tumpati, MD