DUSP28: A Potential Drug Target and Biomarker (G285193)

Target Name: DUSP28

NCBI ID: G285193

DUSP28: A Potential Drug Target and Biomarker

DUSP28 (Dual specificity phosphatase 28) is a protein that is expressed in various tissues of the body, including muscle, liver, and brain. It is a key enzyme in the atidylinositol (PI) signaling pathway, which is involved in a wide range of physiological processes, including muscle contractions, hormone signaling, and neurotransmitter release. In this article, we will discuss DUSP28 as a potential drug target and biomarker.

DUSP28 Structure and Function

DUSP28 is a 28 kDa protein that is localized to the endoplasmic reticulum (ER) and the cytoplasm. It has two distinct active sites that are located in the N-terminus and C-terminus of the protein, respectively. The N-terminus site is involved in the conversion of ATP to ADP, while the C-terminus site is involved in the hydrolysis of the API (adenylylcAMP) to AMP.

DUSP28 is involved in the regulation of several cellular processes, including cell signaling, DNA replication, and protein synthesis. One of its most well-known functions is its role in the regulation of muscle contractions. DUSP28 is known to play a role in the regulation of the myosin ATPase, which is responsible for the production of ATP during muscle contractions.

DUSP28 has also been shown to be involved in the regulation of neurotransmitter release, including the release of synaptic vesicles in neurons. It has also been shown to play a role in the regulation of hormone signaling, including the regulation of insulin sensitivity.

DUSP28 Interactions

DUSP28 has several interactions with other proteins, including:

* DUSP28 can interact with the protein kinase A1 (PKA1) to regulate its activity.
* DUSP28 can interact with the protein kinasePDK1 (PDK1) to regulate its activity.
* DUSP28 can interact with the protein

Protein Name: Dual Specificity Phosphatase 28

Functions: Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate (in vitro) (PubMed:24531476, PubMed:29121083). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine (PubMed:29121083). The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site (PubMed:29121083)

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