AP1S2 Human

Adaptor-related protein complex 1, sigma 2 (AP1S2) is a subunit of the adaptor protein complex 1 (AP-1), which plays a crucial role in the sorting and trafficking of proteins within cells. This complex is essential for the proper functioning of cellular processes, particularly in the late-Golgi/trans-Golgi network (TGN) and endosomes .

The AP-1 complex is a heterotetramer composed of two large adaptins (gamma and beta), one medium adaptin (mu), and one small adaptin (sigma). The sigma subunit, specifically AP1S2, is responsible for recognizing sorting signals within the cytosolic tails of transmembrane cargo molecules . This recognition is vital for the recruitment of clathrin to membranes, facilitating the formation of clathrin-coated vesicles (CCVs) that transport cargo proteins to their designated locations within the cell .

The AP1S2 gene is located on the X chromosome and encodes the sigma 2 subunit of the AP-1 complex. This gene is highly conserved across species, indicating its importance in cellular functions. Alternative splicing of the AP1S2 gene results in multiple transcript variants, which may have distinct roles in different tissues or developmental stages .

Mutations in the AP1S2 gene have been linked to several genetic disorders. One notable condition is Pettigrew syndrome, a form of X-linked intellectual disability characterized by developmental delays, speech impairments, and other neurological symptoms . Additionally, mutations in AP1S2 have been associated with basal ganglia calcification, idiopathic, 6 (IBGC6), a rare neurological disorder that leads to abnormal calcium deposits in the brain .

Human recombinant AP1S2 is used in various research applications to study its role in protein sorting and trafficking. By understanding the function of AP1S2, scientists can gain insights into the molecular mechanisms underlying cellular processes and develop potential therapeutic strategies for related diseases. Recombinant proteins are also valuable tools for investigating the effects of specific mutations and for screening potential drug candidates that target the AP-1 complex.