Receptor-mediated Internalization
Receptor-mediated Internalization - Related Videos
01:56
Internal Receptors
0 Views •
2021
Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas. Similar to membrane-bound receptors, binding of a ligand to a receptor located in the cytoplasm or nucleus of a cell...
01:56
Internal Receptors
0 Views •
2026
Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas. Similar to membrane-bound receptors, binding of a ligand to a receptor located in the cytoplasm or nucleus of a cell...
01:07
Types of Receptors: Internal Receptors
0 Views •
2023
Many cellular signals are hydrophilic and cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind intracellular receptors that reside within the cell cytoplasm or nucleus. Many mammalian steroid hormones and nitric oxide (NO) gas use this cell signaling mechanism. Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...
10:24
Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy
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Cited by 2 •
2017
This protocol describes confocal microscopy detection of G protein-coupled receptor (GPCR) internalization in mammalian cells. It includes the basic cell culture, transfection, and confocal microscopy procedure and provides an efficient and easily interpretable method to detect the subcellular localization and internalization of fusion-expressed GPCR.
01:20
Receptor-Mediated Endocytosis
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2023
Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle. Clathrin-Mediated Endocytosis of LDL One well-characterized example of receptor-mediated endocytosis is the...
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Ligand binding can alter a receptor’s conformation, creating or exposing features that recruit adaptor proteins. These adaptors promote assembly of clathrin-coated pits at the membrane, which enclose the receptor and associated ligand before forming intracellular vesicles. This sequence provides selectivity, allowing particular receptor–ligand complexes to enter the cell rather than undergoing indiscriminate membrane uptake.
After vesicles deliver receptors and their cargo to endosomes, the complexes can follow different outcomes. Receptors may return to the cell surface through recycling, continue to influence signaling from an intracellular location, or proceed toward degradation. These alternatives regulate how long receptors remain available and help cells adjust their responsiveness after ligand exposure.
Conformational changes translate ligand recognition into a trafficking response, while adaptor recruitment links the receptor to the machinery that forms clathrin-coated pits. In neurons, this coupling can alter the number and activity of neurotransmitter or growth-factor receptors at the surface. Consequently, internalization helps regulate signal strength and the capacity of synapses to change.
Examining receptor movement from the cell surface into intracellular compartments can reveal how neuronal signaling is regulated over time. The pattern of recycling, intracellular signaling, or degradation indicates how receptor availability is controlled after ligand binding. These observations help connect altered receptor trafficking with signaling disorders and with changes in synaptic communication or plasticity.
By changing the abundance and activity of receptors at neuronal membranes, internalization can modify how cells respond to neurotransmitters and growth factors. Surface removal may reduce immediate responsiveness, whereas recycling can restore receptor availability. Regulation through these pathways therefore contributes to changing synaptic strength and supports plasticity, the ability of neural connections to adapt.
Drug or toxin binding can alter receptor trafficking and thereby change the duration or intensity of cellular responses. The same selective entry pathway can also provide a route for strategies designed to deliver cargo into cells through receptor recognition. In neuroscience, this relevance extends to understanding cellular barriers and developing approaches that exploit receptor-dependent transport.