The PH domain is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton . This domain can bind phosphatidylinositol lipids within biological membranes, playing a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways .
The FYVE domain is a zinc finger domain that specifically binds phosphatidylinositol 3-phosphate (PI3P), a phosphoinositide found in cellular membranes. This binding is essential for the localization of FYVE domain-containing proteins to endosomal membranes, where they participate in membrane trafficking and signal transduction.
PLEKHF2 is predicted to enable phosphatidylinositol binding activity and is involved in protein transport . It plays a role in early endosome fusion upstream of RAB5, thereby regulating receptor trafficking and fluid-phase transport . Additionally, PLEKHF2 enhances cellular sensitivity to tumor necrosis factor (TNF)-induced apoptosis .
The ability of PLEKHF2 to bind phosphatidylinositol lipids and its involvement in endosomal trafficking highlight its importance in maintaining cellular homeostasis and signaling. Dysregulation of these processes can lead to various diseases, including cancer and neurodegenerative disorders.
Human recombinant PLEKHF2 is used in research to study its role in cellular processes and its potential as a therapeutic target. Understanding the function and regulation of PLEKHF2 can provide insights into the mechanisms of diseases and aid in the development of novel therapeutic strategies.