PPP1R15A: A Potential Drug Target and Biomarker for Protein Phosphatase 1 Regulatory Subunit 15A

Target Name: PPP1R15A

NCBI ID: G23645

PPP1R15A

PPP1R15A: A Potential Drug Target and Biomarker for Protein Phosphatase 1 Regulatory Subunit 15A

Protein phosphatases are a family of enzymes that play a crucial role in cellular signaling pathways. These enzymes remove phosphate groups from protein targets, thereby regulating their activity and localizing them to specific cellular locations. The protein phosphatase 1 (PP1) is a well-known enzyme that is involved in regulating various cellular processes, including cell signaling, cell division, and DNA replication. The regulation of PP1 activity by PP1R15A, a key subunit of PP1, is a critical aspect of its function.

The Protein Phosphatase 1 Regulatory Subunit 15A (PP1R15A)

PP1R15A is a 21-kDa protein that is expressed in various cellular organelles, including the endoplasmic reticulum, endosomal system, and cytoplasm. It plays a critical role in regulating PP1 activity by interacting with the catalytic active site of PP1. This interaction allows PP1R15A to influence the catalytic activity of PP1 and modulate its catalytic efficiency.

PP1R15A functions as a negative regulator of PP1, meaning that it inhibits the activity of PP1. This is achieved by a unique mechanism that involves a direct interaction between PP1R15A and PP1. PP1R15A contains a catalytic active site that is critical for its interaction with PP1. This site is composed of multiple conserved residues, including a lysine residue, which is known as L21. PP1R15A interacts with PP1 through this L21 site, leading to a modulation of PP1 activity.

The PPP1R15A-PP1 Interaction

The PPP1R15A-PP1 interaction is a complex process that involves multiple structural and functional elements. The L21 site of PP1R15A is a key regulatory element that interacts with the active site of PP1. This site is composed of a unique combination of conserved amino acids, including a lysine residue (K21), a proline residue (P21), and a glycine residue (G21).

The interaction between PP1R15A and PP1 is regulated by various factors, including the concentration of PP1 and the presence ofPP1 inhibitors. PP1R15A has been shown to have a regulatory role in cell signaling pathways, including cell proliferation, differentiation, and DNA replication. For instance, PP1R15A has been shown to play a critical role in regulating the growth and differentiation of cancer cells. In addition, PP1R15A has also been shown to play a crucial role in the regulation of cellular responses to various signaling pathways, including the TGF-β pathway.

DPP4 and PP1R15A Interaction

DPP4 (Dipeptidyl-prolyl phosphate) is a protein that is involved in the regulation of protein phosphatases, including PP1. It has been shown to interact with PP1R15A through a unique mechanism that involves a conserved domains between DPP4 and PP1R15A. DPP4 contains a catalytic active site that is critical for its interaction with PP1R15A. This site is composed of multiple conserved amino acids, including a lysine residue (K18), a proline residue (P18), and a glycine residue (G18).

The interaction between DPP4 and PP1R15A is regulated by various factors, including the concentration of DPP4 and the presence of DPP4 inhibitors. DPP4 has been shown to play a critical role in regulating the activity of PP1, including its inhibition of PP1 activity in

Protein Name: Protein Phosphatase 1 Regulatory Subunit 15A

Functions: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress (PubMed:26742780, PubMed:26095357). Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1 (PubMed:14718519). May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15' (PubMed:14635196). Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux (PubMed:32978159). Acts also a viral restriction factor by attenuating HIV-1 replication (PubMed:31778897). Mechanistically, mediates the inhibition of HIV-1 TAR RNA-mediated translation (PubMed:31778897)

The "PPP1R15A Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PPP1R15A comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
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•   expression level;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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