STX12: A Protein Involved in NOTCH and Cytoskeleton Regulation

Target Name: STX12

NCBI ID: G23673

Other Name(s): STX12_HUMAN | Syntaxin-12 | syntaxin 12 | Syntaxin 12 | MGC51957 | STX13 | STX14

STX12: A Protein Involved in NOTCH and Cytoskeleton Regulation

STX12 (STX12_HUMAN) is a protein that is expressed in various tissues of the human body, including the brain, heart, liver, and kidneys. It is a member of the STX12 family, which is characterized by the presence of a unique transmembrane domain and a characteristic N-terminus that is involved in protein-protein interactions.

The STX12 protein is of particular interest as a potential drug target or biomarker due to its involvement in a variety of physiological processes in the body. One of the key functions of STX12 is its role in the regulation of cell adhesion and migration. This protein is known to be involved in the formation of tight junctions, which are a type of cell-cell adhesion that helps to maintain tissue structure and function.

In addition to its role in cell adhesion, STX12 is also involved in the regulation of cell signaling pathways that are critical for various cellular processes, including cell growth, differentiation, and survival. This protein has been shown to play a key role in the regulation of theNotch signaling pathway, which is a well-established regulator of cellular processes that are important for normal development, wound healing, and tissue repair.

The NOTCH signaling pathway is a highly conserved protein that is involved in the regulation of multiple cellular processes, including cell adhesion, stem cell maintenance, and tissue regeneration. The NOTCH signaling pathway is characterized by the presence of a unique N-terminal region that is involved in protein-protein interactions and is thought to play a key role in the regulation of stem cell self-renewal and differentiation.

STX12 is known to be involved in the regulation of NOTCH signaling pathway by its ability to interact with the NOTCH receptor, which is a transmembrane protein that is involved in the regulation of cellular processes that are critical for normal development and survival. The NOTCH receptor is a key regulator of stem cell self-renewal and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders.

The regulation of NOTCH signaling pathway by STX12 is important for understanding the mechanisms of various diseases and for the development of new therapeutic approaches. For example, the deregulation of NOTCH signaling has been implicated in the development of a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders. Therefore, the study of STX12 and its role in the regulation of NOTCH signaling pathway is of great interest and has the potential to lead to new therapeutic approaches for the treatment of these diseases.

In addition to its role in the regulation of NOTCH signaling pathway, STX12 is also involved in the regulation of other cellular processes that are critical for normal development and function. This protein is known to be involved in the regulation of the cytoskeleton, which is the structure that organizes the cytoplasm of cells and is responsible for cell movement and stability.

The cytoskeleton is a complex structure that is composed of a variety of proteins that help to maintain the shape and stability of cells. The cytoskeleton is involved in the regulation of many cellular processes, including cell division, differentiation, and mechanical forces that are exerted by the cell. STX12 is thought to be involved in the regulation of the cytoskeleton by its ability to interact with the microtubules of the

Protein Name: Syntaxin 12

Functions: SNARE promoting fusion of transport vesicles with target membranes. Together with SNARE STX6, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting

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