Cytohesin-2
Cytohesin-2 is a protein that in humans is encoded by the CYTH2 gene. It is a member of the cytohesin family of proteins, which are known to play a crucial role in intracellular signaling and membrane trafficking.
Structure[edit | edit source]
Cytohesin-2 is characterized by the presence of a Sec7 domain, a pleckstrin homology (PH) domain, and a coiled-coil domain. The Sec7 domain is responsible for its guanine nucleotide exchange factor (GEF) activity, which is essential for activating ADP-ribosylation factors (ARFs). The PH domain allows Cytohesin-2 to bind to phosphoinositides in the plasma membrane, facilitating its localization to specific cellular compartments.
Function[edit | edit source]
Cytohesin-2 functions primarily as a GEF for ARFs, small GTP-binding proteins involved in vesicular trafficking. By activating ARFs, Cytohesin-2 regulates various cellular processes, including endocytosis, exocytosis, and actin cytoskeleton remodeling. It is also implicated in signal transduction pathways, influencing cell adhesion, migration, and growth.
Expression[edit | edit source]
The CYTH2 gene is ubiquitously expressed in various tissues, with higher expression levels observed in the brain, heart, and skeletal muscle. The expression of Cytohesin-2 can be regulated by different signaling pathways and is often altered in response to cellular stress or external stimuli.
Clinical Significance[edit | edit source]
Alterations in the expression or function of Cytohesin-2 have been associated with several diseases. For instance, dysregulation of Cytohesin-2 activity has been linked to cancer progression, as it can influence cell migration and invasion. Additionally, Cytohesin-2 has been implicated in neurological disorders due to its significant expression in the brain and its role in neuronal signaling.
Related Proteins[edit | edit source]
Cytohesin-2 is part of a larger family of cytohesins, which includes Cytohesin-1, Cytohesin-3, and Cytohesin-4. These proteins share similar structural domains and functions but may have distinct tissue distributions and specific roles in cellular processes.
See Also[edit | edit source]
- ADP-ribosylation factor
- Guanine nucleotide exchange factor
- Pleckstrin homology domain
- Signal transduction
- Endocytosis
- Exocytosis
References[edit | edit source]
External Links[edit | edit source]
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Contributors: Prab R. Tumpati, MD
