Endocitosis mediada por receptores

Adapter proteins interact with phosphatidylinositol phosphates (PIPs) in the cell membrane to induce conformational changes that expose binding sites for cargo receptors. These proteins facilitate the attachment of clathrin triskelions to the membrane's inner surface, initiating the formation of the clathrin-coated pit and enabling the membrane to curve inward for vesicle formation.

The lower pH inside the endosome causes LDL to dissociate from its receptor protein, the Apo-B receptor. This pH-dependent separation allows intact receptors to be recycled back to the cell membrane for reuse, while LDL remains in the endosome for further processing and breakdown into cholesterol and amino acids.

Clathrin triskelions are protein structures that attach to the inner membrane surface and polymerize to form the clathrin-coated pit. These proteins create a lattice-like coating that gives the budding vesicle its characteristic round shape and helps stabilize the inward membrane curvature necessary for vesicle formation and cargo internalization.

Pathogens like influenza virus and Bacillus anthracis hijack host cell receptors by binding to them on the cell surface. The virus or toxin is then internalized through the cell's native endocytic pathways. Once inside, some pathogens escape the endosome to cause infection, while others release toxins that trigger cellular damage.

Clathrin-mediated endocytosis involves clathrin proteins binding to the outer membrane surface, while caveolin-mediated endocytosis involves caveolin proteins inserting directly into the lipid bilayer. Despite this structural difference, both pathways result in membrane curvature and vesicle formation, though they may internalize different cargo molecules.

Iron enters cells via endocytosis of transferrin, an iron-binding protein that binds to the transferrin receptor (TfR) on the cell surface. A clathrin-coated vesicle forms and transports transferrin into the cell. In the early endosome, decreased pH releases iron from transferrin, while the receptor and empty transferrin are recycled back to the cell surface.

Receptor-mediated endocytosis regulates signaling through sequestration, where signal receptors are internalized and stored in vesicles until needed or degraded by proteolytic enzymes. Additionally, some signaling pathways require endocytosis itself to allow signal transduction to occur, making the process essential for controlling cellular communication and response.