Understanding The Cysteine-Rich Domain of STAC: A Key Protein in Intracellular Signaling

Target Name: STAC

NCBI ID: G6769

STAC

Understanding The Cysteine-Rich Domain of STAC: A Key Protein in Intracellular Signaling

STAC, or SH3-containing protein, is a protein that is expressed in various cell types and is known for its role in intracellular signaling. The protein is composed of a domain that is rich in cysteine 鈥嬧?媟esidues, which is unusual for a protein that is primarily composed of alpha-helices.

The cysteine-rich domain of STAC is thought to play a crucial role in its function. This domain is involved in the formation of a protein-protein interaction (PPI) complex, which is a common structural motif found in proteins that participate in various cellular signaling pathways. The PPI complex is believed to play a key role in the regulation of protein stability, localization, and interactions with other proteins.

In addition to its role in PPIs, the cysteine-rich domain of STAC is also involved in the regulation of protein function. This is done through the formation of a unique structural motif known as a nucleotide-binding oligomerization (NBO) domain. This motif is found in a variety of proteins and is characterized by the presence of a nucleotide base in a specific location that is able to interact with the protein's amino acid side chain.

The NBO domain is believed to function as a molecular chaperone, helping to regulate the stability and localization of other proteins. This is done by the NBO domain's ability to interact with specific amino acids in the target protein, as well as its ability to interact with various nucleotides in the cell's DNA.

One of the unique aspects of the cysteine-rich domain of STAC is its ability to interact with a specific protein called SHC-YAP. SHC-YAP is a protein that is known for its role in the regulation of cell growth, differentiation, and survival . The interaction between STAC and SHC-YAP is thought to be important for the regulation of various cellular processes, including cell proliferation, migration, and invasion.

In addition to its role in the regulation of SHC-YAP function, the cysteine-rich domain of STAC is also involved in the regulation of its own stability. This is done through the formation of a unique structural motif known as a repetitive domain. The motif is found in a variety of proteins and is characterized by the presence of a repeated sequence of amino acids in a specific location.

The repetitive domain is believed to function as a molecular pad, helping to regulate the stability and localization of the protein. This is done by the repetitive domain's ability to interact with specific amino acids in the target protein, as well as its ability to interact with various molecules in the cell's cytoskeleton.

In conclusion, the cysteine-rich domain of STAC is a unique and important protein that is involved in the regulation of various cellular processes. Its role in the formation of PPIs, the regulation of protein function, and the regulation of protein stability makes it an attractive target for drug development. Furthermore, its ability to interact with the protein SHC-YAP and the repetitive domain, suggests that it may be a valuable biomarker for the diagnosis and prognosis of various diseases.

Protein Name: SH3 And Cysteine Rich Domain

Functions: Promotes expression of the ion channel CACNA1H at the cell membrane, and thereby contributes to the regulation of channel activity. Plays a minor and redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. Slows down the inactivation rate of the calcium channel CACNA1C

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