Regulation of Protein Synthesis and Turnover in Eukaryotic Cells

Target Name: GSPT2

NCBI ID: G23708

Regulation of Protein Synthesis and Turnover in Eukaryotic Cells

GSPT2, also known as Eukaryotic peptide chain release factor GTP-binding subunit ERF3B, is a protein that plays a crucial role in the regulation of protein synthesis and turnover in eukaryotic cells. It is a key component of the G-protein-coupled receptor (GPCR) signaling pathway, which is a well-established target for many drugs in the pharmaceutical pipeline.

GSPT2 is a 21-kDa protein that is expressed in most eukaryotic tissues and is highly conserved across different species. It is localized to the endoplasmic reticulum (ER) and is involved in the regulation of protein translation, stability, and degradation. GSPT2 functions as a GPCR-interacting protein, which means that it interacts with GPCR signaling proteins to regulate their activity.

The GPCR signaling pathway is a complex system that involves the interactions of multiple proteins, including GSPT2. It is a critical pathway that regulates many physiological processes in the cell, including sensory perception, neurotransmission, and hormone signaling. The activity of GSPT2 is regulated by various factors, including its own phosphorylation state, which is influenced by factors such as cell stress, growth factors, and signaling pathways.

GSPT2 has been shown to play a critical role in the regulation of protein synthesis and turnover in eukaryotic cells. It is involved in the formation of the endoplasmic reticulum-localized protein transporter TIR, which is critical for the delivery of newly synthesized proteins to the ER for degradation or storage. GSPT2 is also involved in the regulation of protein stability and degradation, which is critical for maintaining the turnover of proteins and for ensuring that cells have access to the latest version of each protein.

GSPT2 has been shown to play a critical role in the regulation of cell signaling pathways. It is involved in the signaling pathways that regulate cell adhesion, migration, and survival. GSPT2 has been shown to interact with various signaling proteins, including the T-cell receptor (TCR), which is critical for the regulation of cell differentiation and immune responses.

GSPT2 has also been shown to play a critical role in the regulation of cell cycle progression. It is involved in the regulation of protein synthesis and degradation during the G1 phase of the cell cycle, which is critical for cell growth and progression. GSPT2 has been shown to interact with the cyclin D1 protein, which is critical for the regulation of cell cycle progression.

In conclusion, GSPT2 is a protein that plays a critical role in the regulation of protein synthesis and turnover in eukaryotic cells. Its activity is regulated by various factors, including its own phosphorylation state, which is influenced by factors such as cell stress, growth factors, and signaling pathways. GSPT2 is involved in the formation of the endoplasmic reticulum-localized protein transporter TIR and is also involved in the regulation of cell signaling pathways, cell adhesion, migration, and survival. It is potential drug target or biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

Protein Name: G1 To S Phase Transition 2

Functions: Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons

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