Rabbit Anti-AP2M1 Polyclonal Antibody#abs136481

abs136481-100ug

1-2 Weeks

301.0

abs136481-50ug

1-2 Weeks

201.0

catalog

Description

The role of the AP-2 coat assembly protein complex cannot be understated in receptor-mediated endocytosis at the plasma membrane. This complex, composed of α, β, μ, and σ protein subunits, forms clathrin-coated pits essential for cellular internalization (1-3). Within this complex, the 50 kDa μ subunit (AP-2μ, AP2M1) takes center stage as it mediates the interaction between cargo proteins and the clathrin-coated pit (1-4). By recognizing the tyrosine-based endocytotic sorting motif YXXφ, located at the carboxy-terminal AP2M1 region, it efficiently directs cargo proteins to the clathrin-coated pit (1-4). However, it's worth noting that non-canonical tyrosine-based endocytotic sorting signals can also facilitate the interaction between cargo proteins and AP2M1 (5,6).
Not limited to internalization processes alone, AP2M1 displays its versatility by participating in molecular signaling pathways involving membrane receptors, matrix metalloproteinases, and ion channel proteins (7-11). This adaptability is integral in coupling receptor-mediated endocytosis with these varied pathways, highlighting its role as a molecular mediator (7-11). Additionally, AP2M1 activity can be modulated by the phosphorylation of specific AP2M1 residues and the binding of lipids to the protein (12,13). For instance, the phosphorylation of AP2M1 at Thr156 by adaptor-associated kinase 1 (AAK1) can enhance the affinity binding of AP2M1 to cargo protein signals (14).
Overall, the AP-2 coat assembly protein complex, with its aforementioned component AP2M1, holds a critical position in cellular processes, bridging receptor-mediated endocytosis and various signaling cascades through its ability to recognize sorting motifs and adjust its activity through phosphorylation and lipid interactions (1-14).

Concentration

1mg/ml

Target

Background

Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity).