Abstract
Clathrin-mediated endocytosis (CME) is a fundamental process for the regulated internalization of transmembrane cargo and ligands via the formation of vesicles using a clathrin coat. A vesicle coat is initially created at the plasma membrane by clathrin assembly into a lattice, while a specific cargo sorting process selects and concentrates proteins for inclusion in the new vesicle. Vesicles formed via CME traffic to different parts of the cell and fuse with target membranes to deliver cargo. Both clathrin assembly and cargo sorting functions are features of the two gene family consisting of assembly protein 180 kDa (AP180) and clathrin assembly lymphoid myeloid leukemia protein (CALM). In this review, we compare the primary structure and domain organization of CALM and AP180 and relate these properties to known functions and roles in CME and disease.
Highlights
Clathrin mediated endocytosis (CME) is a fundamental multi-functional biological process
There is a lack of mechanistic detail and some unanswered questions about clathrin assembly lymphoid myeloid leukemia protein (CALM) and assembly protein 180 kDa (AP180) function
In what order do clathrin and adaptor protein complex 2 (AP2) interact with CALM and AP180? Many clathrin binding sites on AP180 and some for CALM have been identified, but what is the mechanism of assembly and how are uniform vesicles achieved? Approaches that allow an acute knockout/knockdown or single molecule resolution analysis of CALM and AP180 may provide this detail
Summary
Clathrin mediated endocytosis (CME) is a fundamental multi-functional biological process. These functions include the internalization of receptors, recycling of membrane components, internalization of toxins and viruses, nutrient uptake and activation of signaling pathways including those controlling. Vesicles produced by CME or synaptic vesicle endocytosis (SVE) [3] must include proteins for targeting and fusion of the vesicle with the correct intracellular membranes [4]. A major difference between vesicles made by CME and SVE is that SVs are smaller in diameter, which is likely due to mechanistic differences in how adapter proteins sort cargo and assemble the clathrin coat [1,5]. We will relate their sequence similarities and differences to their known functions
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