Unlocking the Potential of PPP1R12A: A Druggable Myosin-Binding Subunit for Parkinson's Disease

Target Name: PPP1R12A

NCBI ID: G4659

Unlocking the Potential of PPP1R12A: A Druggable Myosin-Binding Subunit for Parkinson's Disease

Introduction

Parkinson's disease is a neurodegenerative disorder characterized by motor symptoms such as tremors, rigidity, and bradykinesia. The most common cause of Parkinson's disease is the loss of dopamine-producing neurons in the brain, leading to a decline in motor function. Although numerous medications have has been developed to treat Parkinson's disease, the disease remains a significant public health burden due to its progressive and debilitating effects. Therefore, there is a growing interest in identifying new drug targets and biomarkers for the development of more effective therapies.

PPP1R12A, a protein phosphatase myosin-binding subunit, has emerged as a promising drug target and biomarker for the treatment of Parkinson's disease. PPP1R12A is a key component of the protein complex known as the endoplasmic reticulum (ER) and plays a critical role in regulating the activity of myosin, which is the protein responsible for muscle contraction. The loss of PPP1R12A has been linked to the dysfunction of the myosin-endoplasmic reticulum (MER) complex, which is responsible for maintaining the integrity of the ER and the proper functioning of the myosin network.

The Myosin-Binding Subunit (MBS)

Myosin is a protein that plays a central role in muscle contraction and relaxation. It consists of several subunits, including M1, M2, M3, and M4, which are involved in the regulation of the myosin ATPase complex. Myosin is also known as myosin Protein and has a critical role in the regulation of muscle strength and function.

The PPP1R12A is a protein phosphatase myosin-binding subunit that is expressed in various tissues, including muscle, brain, and heart. It is involved in the regulation of myosin function and has been shown to play a critical role in the regulation of muscle contraction and relaxation.

The Endoplasmic Reticulum

The endoplasmic reticulum (ER) is a series of membrane systems wrapped in the cytoplasmic membrane, including rough endoplasmic reticulum (cytoskeleton) and smooth endoplasmic reticulum (smooth endoplasmic reticulum) ). 锛? 锛?

The ER is a series of membrane systems wrapped in the cytoplasmic membrane, including rough endoplasmic reticulum (cytoskeleton) and smooth endoplasmic reticulum (smooth endoplasmic reticulum). 锛? 锛? The ER is responsible for the synthesis, processing, and storage of proteins, as well as the modification and degradation of these proteins. The ER also plays a critical role in the regulation of intracellular signaling pathways and is involved in the regulation of various cellular processes , including cell growth, differentiation, and stress response.

The Myosin-Endoplasmic Reticulum (MER) Complex

The Myosin-Endoplasmic Reticulum (MER) complex is a protein complex that is responsible for the regulation of myosin function. The MER complex consists of several subunits, including PPP1R12A, which is involved in the regulation of myosin ATPase complex.

PPP1R12A is a protein phosphatase myosin-binding subunit that is expressed in various tissues, including muscle, brain, and heart. It is involved in the regulation of myosin function and has been shown to play a critical role in the regulation of muscle contraction and relaxation.

The Loss of PPP1R12A

The loss of PPP1R12A has been linked to the dysfunction of the

Protein Name: Protein Phosphatase 1 Regulatory Subunit 12A

Functions: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity

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