SUMO1: A Key Regulator of GPCR and Cellular Signaling Pathways

Target Name: SUMO1

NCBI ID: G7341

SUMO1

SUMO1: A Key Regulator of GPCR and Cellular Signaling Pathways

SUMO1 (GAP-modifying protein 1) is a protein that plays a critical role in various cellular processes, including cell division, apoptosis, and signaling pathways. It is a key regulator of the G-protein-coupled receptor (GPCR) signaling pathway, which is involved in many cellular processes, including sensory perception, neurotransmission, and hormone signaling. SUMO1 is also involved in the regulation of cell cycle progression, and has been shown to play a role in the regulation of cell growth, apoptosis, and cancer progression.

SUMO1 is a protein that is expressed in many different tissues and cells, including neurons, cardiac muscle cells, and cancer cells. It is primarily localized to the endoplasmic reticulum (ER), a system of organelles that transports and modifies proteins before they are released into the cytosol for further processing. SUMO1 is also known to be involved in the regulation of protein stability and localization to the ER, as well as in the regulation of cellular signaling pathways.

One of the key functions of SUMO1 is its role as a GPCR regulator. GPCRs are a family of transmembrane proteins that are involved in the regulation of cellular signaling pathways, including sensory perception, neurotransmission, and hormone signaling. SUMO1 is shown to play a critical role in the regulation of GPCR signaling by modifying the activity of GPCRs. This modification allows SUMO1 to regulate the activity of GPCRs in a targeted and efficient manner, which is essential for the regulation of cellular signaling pathways.

SUMO1 is also involved in the regulation of cell cycle progression, which is the process by which cells grow, divide, and replicate their genetic material. SUMO1 is shown to play a critical role in the regulation of cell cycle progression by modifying the activity of the microtubule protein T-complex. T-complex is a protein that plays a critical role in the regulation of cell division, and is composed of the protein T-tubulin and the protein microtubule protein (MAPK) 1. SUMO1 is shown to regulate the activity of T-complex by modifying the activity of MAPK 1, which is a protein that is involved in the regulation of cellular signaling pathways.

In addition to its role as a GPCR regulator and cell cycle regulator, SUMO1 is also involved in the regulation of apoptosis, which is the process by which cells die and are removed from the body. SUMO1 is shown to play a critical role in the regulation of apoptosis by modifying the activity of the protein B-cell lymphoma 1 (Bcl-1). Bcl-1 is a protein that is involved in the regulation of apoptosis, and is shown to be regulated by SUMO1.

SUMO1 is also involved in the regulation of many other cellular processes, including cell adhesion, migration, and angiogenesis. It is also involved in the regulation of inflammation, and is shown to play a role in the regulation of the immune response.

In conclusion, SUMO1 is a protein that plays a critical role in various cellular processes, including cell division, apoptosis, and signaling pathways. It is a key regulator of the G-protein-coupled receptor (GPCR) signaling pathway, and is involved in the regulation of GPCR activity, cell cycle progression, apoptosis, and many other cellular processes. SUMO1 is also shown to play a role in the regulation of cell adhesion, migration, and angiogenesis, as well as in the regulation of inflammation. Given its involvement in these critical cellular processes, SUMO1 is a potential drug target and biomarker for a variety of diseases.

Protein Name: Small Ubiquitin Like Modifier 1

Functions: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376)

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