FRMPD3

FRMPD3 is a human gene that encodes a protein, also referred to as FRMPD3. It belongs to the FERM domain-containing protein family.

Function:

The precise function of the FRMPD3 protein is not fully understood, but it is believed to play a role in cellular signaling and adhesion. FERM domains are protein modules found in a variety of proteins involved in linking transmembrane proteins to the cytoskeleton. They typically bind to integral membrane proteins and phosphoinositides, facilitating protein complex assembly at the cell membrane. Therefore, FRMPD3 is likely involved in similar processes. Specific roles in neuronal development and synapse formation have been suggested, though more research is needed to confirm these hypotheses.

Structure:

The FRMPD3 protein contains a FERM domain, characteristic of proteins in this family. The FERM domain is composed of three subdomains (F1, F2, and F3) that interact to form a globular structure. These subdomains mediate interactions with various ligands, including membrane proteins and lipids. The specific structure of FRMPD3 contributes to its binding affinity and selectivity for its interacting partners.

Expression:

FRMPD3 is expressed in various tissues, including the brain. Studies suggest specific expression patterns in certain brain regions, hinting at a potential role in neural function. Its expression levels can vary during development and in different cell types.

Clinical Significance:

Although not definitively linked to specific diseases currently, altered expression or mutations in the FRMPD3 gene may be associated with neurological disorders. Ongoing research is exploring its potential involvement in conditions where synaptic dysfunction or impaired cellular adhesion are implicated. The FRMPD3 gene resides on chromosome 3.

Further Research:

Further research is necessary to fully elucidate the function of FRMPD3, its interacting partners, and its role in human health and disease. Studies focusing on its involvement in cellular signaling pathways, its interactions with other proteins, and the effects of genetic variations are needed.