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Alpha and Gamma-Adaptin Binding Protein (AAGAB), also known as p34, is a protein encoded by the AAGAB gene. This protein interacts with the alpha- and gamma-adaptin subunits of clathrin adaptor protein complexes, which are crucial for clathrin-mediated vesicle trafficking . Clathrin-mediated endocytosis is a fundamental cellular process that facilitates the internalization of various molecules, including nutrients, hormones, and other signaling molecules .
The AAGAB gene is located on chromosome 15 and encodes a protein that is approximately 34 kDa in size . The protein is predominantly cytosolic and is involved in the regulation of clathrin adaptor protein complexes AP1 and AP2 . These complexes play a pivotal role in the formation of clathrin-coated vesicles, which are essential for intracellular trafficking between the plasma membrane, trans-Golgi network, and endosomes .
AAGAB functions as an assembly chaperone for the AP1 and AP2 clathrin adaptor complexes . It binds to and stabilizes the gamma and alpha subunits of these complexes, promoting their assembly and function. This stabilization is crucial for the proper sorting and trafficking of cargo proteins within the cell . Mutations in the AAGAB gene can disrupt this process, leading to various cellular dysfunctions and diseases .
Mutations in the AAGAB gene are associated with type I punctate palmoplantar keratoderma, a skin disorder characterized by the development of hyperkeratotic lesions on the palms and soles . Additionally, AAGAB has been identified as a potential biomarker for certain cancers, including breast cancer . Its expression levels can influence the response to neoadjuvant chemotherapy, making it a valuable target for diagnostic and prognostic applications .
Recent studies have highlighted the importance of AAGAB in maintaining cellular homeostasis and its potential role in disease pathogenesis . Understanding the molecular mechanisms underlying AAGAB function can provide insights into the development of therapeutic strategies for diseases associated with clathrin-mediated trafficking defects .