Moving Components Through the Cell

William Stillwell , in An Introduction to Biological Membranes (2d Edition), 2016

3 Receptor-Mediated Endocytosis

RME [11,12] is besides known as clathrin-dependent endocytosis because of involvement of the membrane-associated protein clathrin in forming membrane vesicles that become internalized into the jail cell. Clathrin plays a major office in formation of clathrin-coated pits and coated vesicles. Since clathrin was first isolated and named by Barbara Pearse in 1975 [thirteen], it has become clear that clathrin and other coat proteins play essential roles in prison cell biology. Clathrin is an essential component in edifice small vesicles for uptake (endocytosis) and consign (exocytosis) of many molecules. While the methods of membrane send, discussed in Chapter 19, involved minor solutes, RME is the main mechanism for the specific internalization of most macromolecules by eukaryotic cells.

RME begins with an external ligand bounden to a specific receptor that spans the plasma membrane (Fig. 17.3, [14,15]). Examples of these ligands include hormones, growth factors, enzymes, serum proteins, low-density lipoprotein (LDL) (with attached cholesterol), transferrin (with attached iron), antibodies, some viruses, and even bacterial toxins. Afterward receptor binding, the circuitous diffuses laterally in the plasma membrane until it encounters a specialized patch of membrane called a coated pit. The receptor–ligand complexes accumulate in these patches as practise other proteins including clathrin, adaptor protein, and dynamin. Since coated pits occupy about 20% of the plasma membrane surface surface area, they are non pocket-sized membrane features. The collection of these proteins starts to curve the adjacent section of the membrane that eventually pinches off to form an internalized coated vesicle. Clathrin and dynamin then recycle back to the plasma membrane, leaving an uncoated vesicle that is free to fuse with an early endosome. Later the early endosomes mature into late endosomes, they and so go to the lysosome for digestion. RME is a very fast process. Invagination and vesicle formation take about ane   min. I single cultured fibloblast cell can produce 2500 coated pits per minute.

Figure 17.iii. Receptor mediated endocytosis (also known as clathrin-dependent endocytosis).

 Reference Grant BD, Sato G. http://world wide web.wormbook.org/chapters/www_intracellulartrafficking/intracellulartrafficking.html; 2006.

One instance of RME has received a slap-up deal of attending because of its essential role in human health, namely maintaining the proper level of cholesterol in the body. Malfunctions in the RME procedure for uptake of cholesterol-carrying LDL (run into Affiliate xiv) leads to hypercholesterolemia and cardiovascular disease [11,16]. RME and its role in cholesterol metabolism was discovered by Michael Brownish and Joseph Goldstein of The Academy of Texas Health Science Middle in Dallas (at present the UT Southwestern Medical Center), who received the 1985 Nobel Prize in Physiology and Medicine for their iconic piece of work.

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A new approach for drug targeting to the central nervous system

Berrin Küçüktürkmen , Asuman Bozkır , in Nanoarchitectonics in Biomedicine, 2019

ten.two.ii.vi Receptor-mediated endocytosis

Receptor-mediated endocytosis occurs with the bounden of ligands to the specific receptors located in the luminal membrane of the BBB. In that location are many endogenous ship systems in the BBB. For example, glucose, which is the major energy source of the brain is transported by glucose transporter-1 receptor, while aminoacids are transported past the l-type aminoacid transporter-1 receptor. Thiamin, biotin, folic acid, vitamin B12, Tf, and neuropeptides are transported by their respective specific receptors, while insulin-like growth factors IGF-I and IGF-II and leptin are transported by the endogenous receptors located in the brain vascular endothelium constituting the BBB (Punitha and Srivastava, 2013). The receptor-mediated endocytosis systems used to administer agile ingredients to the brain are based on both endogenous and chimeric ligands. Insulin, Tf, and folic acid are endogenous ligands with loftier affinity for brain and tumor cells. Their biocompatibility and nonimmunologic nature are advantageous. Insulin has some disadvantages such as its short half-life and causing hypoglycemia at loftier concentrations. Tf is a monomeric glycoprotein that can carry one or two atomic number 26 atoms. It is highly expressed in brain capillary endothelium and the surfaces of some rapidly reproducing cells similar tumor cells of the encephalon (Beduneau et al., 2007). Folic acid receptors are usually expressed in brain and choroid plexus cells. Folic acid receptors are expressed particularly in near cancer cells originating from the epithelium and play an important role in the survival and reproduction of cells (Punitha and Srivastava, 2013). Therefore, targeting drugs to folic acid receptors specially in oncologic diseases is promising.

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Virus Replication

Jennifer Louten , in Essential Human Virology, 2016

4.ii Penetration

Following attachment, successful viruses apace gain entry into the prison cell to avoid extracellular stresses that could remove the virion, such every bit the menses of mucus. Penetration refers to the crossing of the plasma membrane past the virus. In contrast to virus zipper, penetration requires energy, although this is contributed past the host prison cell, non the virus.

Several different mechanisms are utilized past viruses to gain entry into a prison cell (Fig. 4.4, Table 4.two). One of these takes advantage of a normal host process: endocytosis. As described in Chapter 3, "Features of Host Cells: Cellular and Molecular Biology Review," cells are able to import molecules through the process of endocytosis. Receptor-mediated endocytosis occurs when receptors on the prison cell surface are bound by their ligands and internalized in clathrin-coated pits or caveolae that become endocytic vesicles. Eventually, these vesicles lose their clathrin or caveolin coating and fuse with "early endosomes," slightly acidic vesicles (pH of 6.0–6.5) that get "tardily endosomes" equally their acidity increases (pH of 5.0–half-dozen.0). Late endosomes deliver materials to lysosomes, larger vesicles full of digestive enzymes.

Figure 4.4. Viral penetration into the prison cell.

Unlike viruses have advantage of diverse cellular mechanisms to gain entry into the cell subsequently binding their specific jail cell surface receptors. Some enveloped viruses undergo fusion, which fuses the viral envelope with the plasma membrane. Both enveloped and nonenveloped viruses take advantage of receptor-mediated endocytosis in caveolin- or clathrin-coated pits to proceeds entry into the cytoplasm of the prison cell. Nonetheless other viruses undergo receptor-mediated endocytosis that is contained of both clathrin and caveolin. Bulk-phase endocytosis and phagocytosis are also utilized by viruses to gain entry into the cell.

Table 4.ii. Methods of Penetration for Select Human being Viruses

Type of penetration (entry) Virus examples
Clathrin-mediated endocytosis Dengue virus, hepatitis C virus, reovirus, adenovirus, parvovirus B19, West Nile virus
Caveolin-mediated endocytosis Human papillomavirus, SV40, hepatitis B virus
Fusion HIV, flu, respiratory syncytial virus, herpes simplex viruses, dengue virus, Ebola virus

Receptor-mediated endocytosis is commonly used by viruses to penetrate the plasma membrane. As the pH of the endosome drops, the viral proteins change configuration, which allows them to escape from the endosome. Depending upon the virus, this can happen in early endosomes, belatedly endosomes, or lysosomes. Both enveloped and nonenveloped viruses have reward of receptor-mediated endocytosis to proceeds entry into the cytoplasm of the jail cell (Fig. four.four). Most types of viruses utilize clathrin-mediated endocytosis to enter the cell, including dengue virus, hepatitis C virus, and reoviruses. A few well-known viruses that infect humans, such as SV40 and papillomaviruses (that cause warts or cervical cancer), use caveolae-mediated endocytosis; this was discovered by using a drug that inhibited the formation of caveolae. Blocking clathrin-mediated endocytosis did not prevent

In-Depth Expect: Tropism

Different cells perform different functions within a multicellular organism. As such, not all cells within the body brandish the same types of cell surface proteins. The tropism of a virus refers to the specificity of a virus for a particular host cell or tissue. Viruses will merely be able to infect the cells that display the molecules to which their virus attachment proteins bind. Similarly, one reason that certain viruses accept a narrow host range is because unlike host species may lack the cell surface proteins that a detail virus uses for attachment. For instance, humans are the only known natural hosts of poliovirus. Because of this, poliovirus has historically been a hard virus to study because the cell surface receptor it uses for attachment, called CD155 or the poliovirus receptor, is not present in modest fauna models, such as mice. In 1990, a transgenic mouse strain was engineered to express the homo CD155 molecule. These mice were susceptible to infection, whereas the normal nontransgenic mice were non (Fig. iv.3).

Effigy 4.three. Transgenic mice for the homo poliovirus receptor CD155.

In 1990, the Racaniello enquiry group generated mice that expressed human CD155, the poliovirus receptor. Poliovirus does not replicate in normal mice because they lack this receptor. When the CD155-transgenic mice were infected intracerebrally with poliovirus, the virus replicated in the brain and spinal cord, causing paralysis. These transgenic mice have proved useful in studying poliovirus infection in a nonprimate animal model.

 (Study documented in Ren et al., 2012. Cell 63(2), 353–362.)

the entry of these viruses into cells. Still other viruses undergo receptor-mediated endocytosis that is independent of both clathrin and caveolin.

Other forms of endocytosis, such every bit majority-phase endocytosis and phagocytosis, are also exploited past viruses to enter the jail cell. In bulk-stage endocytosis, the jail cell forms a vesicle that engulfs whatever molecules are present in the extracellular fluid, including viruses. Phagocytosis is a form of receptor-mediated endocytosis that is used by specialized cells to engulf unabridged cells. Recently, 2 big DNA viruses, HSV-one and mimivirus, were shown to enter cells through phagocytosis-like pathways.

A method of penetration that is used exclusively by enveloped viruses is fusion. Fusion of the viral envelope can occur at the prison cell membrane or within endocytosed vesicles, such as the endosome, and is mediated by the same viral protein that is used by the virus for attachment or by a different viral protein, depending upon the virus. For instance, HIV has a protein known as gp120 that binds to CD4 and one of the two coreceptors for entry, CCR5 or CXCR4. Once this occurs, a unlike viral protein, gp41, fuses the virus envelope with the cell membrane, releasing the nucleocapsid into the cytoplasm.

Study Break

Describe the dissimilar ways that viruses can gain entry into the cytosol.

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Dendrimers as Effective Carriers for the Treatment of Brain Tumor

Bapi Gorain , ... Prashant Kesharwani , in Nanotechnology-Based Targeted Drug Delivery Systems for Encephalon Tumors, 2018

ten.3.2.2 Insulin Receptor

Receptor-mediated endocytosis into the brain could too be possible through this insulin receptor present in endothelial cells. This insulin receptor is a tyrosine kinase heterotetramer receptor containing two extracellular α- and two transmembrane β-subunits. The β-subunits are continued to cytosolic tyrosine kinase ( de Boer & Gaillard, 2007). Pardridge et al. have extensively studied insulin receptors of the brain using specific antibiotic targeting to insulin receptors. Thus, ligand binding to the targeted insulin receptor resulted in receptor activation through autophosphorylation and was followed past internalization of the receptor–ligand complex (Boado, Zhang, Zhang, & Pardridge, 2007; Orthmann et al., 2011; Pardridge, 2010, 2015). Ulbrich et al. reported that a homo serum albumin-loaded nanocarrier coupled with an antiinsulin receptor monoclonal antibiotic could be an constructive delivery organisation to transport loperamide beyond the BBB, as evidenced by the significant antinociceptive activeness in the tail-flick experiment. Loperamide is unremarkably unable to cantankerous the BBB, whereas this conjugation of loperamide nanocarrier with antiinsulin monoclonal antibody assisted in delivering the drug at a therapeutic concentration to the brain (Ulbrich, Knobloch, & Kreuter, 2011).

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Functional Moieties for Intracellular Traffic of Nanomaterials

Ana L. Silva , ... Helena F. Florindo , in Biomedical Applications of Functionalized Nanomaterials, 2018

2.1.ane Clathrin-Mediated Endocytosis

Receptor-mediated endocytosis is often assisted by vesicles' coating with proteins, such as clathrin and caveolin-1 ( Paulo et al., 2011). CME is the "classical route" of internalization for macromolecules and for nearly cell types (Bareford and Swaan, 2007). It is responsible for the uptake of essential nutrients, such equally cholesterol past low-density lipoprotein (LDL) particles via the LDL receptor or iron-loaded transferrin (Tf) via the Tf receptor (TfR) (Sahay et al., 2010a). CME is mediated by the production of small vesicles coated past clathrin that forms domains of the plasma membrane termed clathrin-coated pits. Clathrin-coated vesicles may take sizes ranging from 50 to 300   nm, and the particulate matter reported to be internalized by CME presents mostly up to 200   nm in bore (Andersen et al., 2014). After internalization, clathrin is uncoated and the vesicles fuse together to course early endosomes, where sorting occurs to later compartments. Endocytosed material may be transported to the late endosomes and lysosomes for degradation, to the trans-Golgi network, or recycled to the prison cell surface (Ferrati et al., 2011; Paulo et al., 2011). Mature endosomal compartments fuse with lysosomal vesicles and continuously acidify from the original neutral pH on the cell surface to pH 4.8 in the lysosomes, resulting in the enzymatic destruction of a variety of molecules, including lipids, carbohydrates, nucleic acids, and viruses (Bareford and Swaan, 2007).

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Antimicrobial Nanostructures for Neurodegenerative Infections

Arunachalam Muthuraman , Jaspreet Kaur , in Nanostructures for Antimicrobial Therapy, 2017

6.2 Cellular Receptor–Mediated Endocytosis

Receptor-mediated endocytosis has potential selectivity in the entry of molecules into cellular target sites. The nanoparticle surface binds to the extracellular surface and the cell allows carrying the ligands into the cytosolic region ( Wang et al., 2012a). Sometimes, it transduces the signal to the intracellular space and triggers various biochemical pathways. Furthermore, it may also enhance the internalization of the ligand and its nanoparticle via the endocytosis process. This process is potentiated past biomolecules such every bit caveolin and clathrin (Rattanapinyopituk et al., 2014; Smith et al., 2012). The cross-linking of receptors and nanoparticles is more prone to membrane enfolding and reunification leading to the formation of an endosome. Nanoparticles between 25 and l   nm in size are involved in this kind of entry into the cellular arrangement (El-Sayed and Harashima, 2013; Steketee et al., 2011). Cellular endocytosis follows five steps to carry the nanoparticle with ligands into the cytosolic region. The steps are as follows: (1) clan of nanoparticles with receptors on the cell membrane, (2) internalization of nanoparticles with ligands, (3) release of ligands (also known as endosomal escape) from nanoparticles by the endolysosomal procedure or lysosomal degradation of nanoparticles, (four) interaction of costless ligands (therapeutic amanuensis) with cytoplasmic organelles or proteins, and (five) exocytosis of nanoparticles via the endosomal recycling process (Xu et al., 2013; Herd et al., 2013; Serda et al., 2010; Strobel et al., 2015). A summary of nanoparticle entry and emptying in the cellular system is illustrated in Fig. 6.2.

Effigy six.2. The process of nanomedicine entry and elimination of nanoparticles in the cellular organisation. Information technology has five major steps, i.eastward., (1) association of nanoparticle with cellular membrane, (ii) internalization of endosomal circuitous, (iii) endolysosomal or lysosomal deposition, (4) release of drug and activation at targeted site, and (5) release of nanoparticles from cellular system by exocytosis with endosome.

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Protein Synthesis, Processing, and Trafficking

Randal J. Kaufman , Laura Popolo , in Hematology (Seventh Edition), 2018

Receptor-Mediated Endocytosis

Receptor-mediated endocytosis is a means to import macromolecules from the extracellular fluid. More than 20 different receptors are internalized through this pathway. Some receptors are internalized continuously whereas others remain on the surface until a ligand is bound. In either case, the receptors slide laterally into coated pits that are invaginated regions of the plasma membrane surrounded by clathrin and pinch off to form clathrin-coated vesicles. The immediate destination of these vesicles is the endosome.

The endosome is part of a complex network of interrelated membranous vesicles and tubules termed the endolysosomal arrangement. The endolysosomal system comprises four types of membrane-spring structures: early endosomes (EEs), belatedly endosomes (LEs), recycling vesicles, and lysosomes. It is still a matter of debate whether these structures represent contained stable compartments or one structure matures into the adjacent. The interior of the endosomes is acidic (pH about 6). Endocytosed material is ultimately delivered to the lysosome, presumably by fusion with LE. Lysosomes also assimilate obsolete parts of the cell in a procedure called autophagy.

During the formation of clathrin-coated vesicles, clathrin molecules do not recognize cargo receptors straight merely rather through the adaptor proteins, that form an inner glaze. The AP-two components demark both clathrin and sorting signals present in the cytoplasmic tails of cargo receptors shut to the plasma membrane. These internalization motifs are: YXXϕ (where ϕ is a hydrophobic amino acrid), as a virtually common motif, and the NPXY bespeak that was get-go identified in the LDL receptor. For receptors that are internalized in response to ligand bounden, the internalization signal may too be generated by a conformational change induced past the binding of the ligand. Through the specificity of the AP-2 circuitous, the capture of a unique prepare of cargo receptors is linked to vesiculation resulting in concentration of the cargo. The coated pit pinches off from the plasma membrane by the action of a GTP-binding protein, dynamin, which forms a band around the cervix of each bud and contributes to the vesicle formation. Later release and shedding of the clathrin glaze, the vesicle fuses with the EE compartment.

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Molecular, functional, and evolutionary aspects of ADP-ribosylating toxins

Vega Masignani , ... Rino Rappuoli , in The Comprehensive Sourcebook of Bacterial Protein Toxins (Third Edition), 2006

Receptor-mediated endocytosis

Receptor-mediated endocytosis is used past soluble toxins with an A/B structure and by binary toxins where the A and B domains are physically separated. The toxins with this construction are released by leaner in the culture supernatant and bind to the surface of eukaryotic cells by their B domain, which contains a receptor-bounden site. Following binding, the A/B toxins are internalized and located in membrane-bound vesicles (early endosomes). In the case of binary toxins, the B domain binds kickoff to the cell receptor and so captures the A domain to the cell surface. The binding components of C2 toxin and iota toxin have been shown to form heptamers in solution ( Barth et al., 2000; Blocker et al., 2001). In the instance of C2, once formed, the heptamers insert as pores into the lipid bilayer and mediate the translocation of the agile subunit into the cytosol (Blocker et al., 2003). Furthermore, the host cell chaperone Hsp90 has recently been shown to be essential in the second step of translocation of C2I and iota toxin from endosomes into the cytosol (Haug et al., 2004). Post-obit internalization, 2 quite different pathways are used by different toxins to translocate their A domain into the cytosol. The ii pathways take been best studied for diphtheria and cholera toxin, respectively. Diphtheria toxin A domain crosses the membrane early later internalization (see Figure 12.4, path 1). As soon as the pH of the endosomes decreases to 5.5 units, the B domain changes conformation and exposes hydrophobic α-helices that are not soluble any longer in h2o and therefore penetrate the lipid bilayer of the membrane. This initiates a process that favors the translocation of the A subunit across the membrane and too involves the activity of a cytosolic translocation factor (TFC) complex. (See the paragraph on diphtheria toxin for a more detailed description of this process.)

The toxins known to cantankerous the membrane by a mechanism similar to diphtheria toxin are botulinum and tetanus toxins.

Conversely, cholera toxin has a much more than complicated intracellular route before information technology reaches the cytoplasm (Figure 12.4, path ii). Following internalization in early on endosomes, it undergoes a retrograde ship back to the Golgi apparatus, across it until it reaches the endoplasmic reticulum (ER). The routing of the A subunit to this pathway is believed to exist mediated by an amino acid motif (KDEL), which is similar to the endoplasmic reticulum retention domain of eukaryotic proteins. One time in the ER, the misfolded catalytic toxin subunit uses a retro-translocation path to finally reach the cytosolic compartment, where it rapidly refolds, avoids the proteasome, and induces toxicity (Lencer and Tsai, 2003).

The toxins that follow the intracellular road of cholera toxin are: Shiga toxin, the related verotoxin, pertussis toxin, E. coli heat-labile enterotoxin, and Pseudomonas exotoxin A (Johannes and Goud, 1998).

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Innate Immunity

Tak W. Mak , Mary Eastward. Saunders , in The Immune Response, 2006

two) Receptor-Mediated Endocytosis

In receptor-mediated endocytosis (Fig. 4-3B), uptake of the foreign macromolecule depends on its interaction as a soluble ligand with an appropriate receptor on the surface of the endocytic jail cell. Bounden of the macromolecule to a receptor triggers the polymerization of clathrin, a protein component of the microtubule network located on the cytoplasmic side of the plasma membrane. Invagination of clathrin-coated "pits" internalizes the receptor and its spring foreign ligand into a "coated" vesicle of a size in the range of 0.xv–0.45 μm. Clathrin-coated vesicles are much more than uniform in size than those created by macropinocytosis.

The uptake of foreign materials by the mechanisms of macropinocytosis and receptor-mediated endocytosis does more than simply sequester antigens: internalization also initiates the processing of these antigens that leads to recognition by cells of the adaptive immune system, another example of the inextricable linkage of the innate and adaptive responses.

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Endosomal escape tendency of drug delivery systems to mediate cytosolic commitment of therapeutics

Sandeep Kaur Bansal , ... Rakesh K. Tekade , in The Time to come of Pharmaceutical Product Development and Research, 2020

7.ii.1.1.1 Clathrin-dependent endocytosis

Most receptor-mediated endocytosis is clathrin-dependent and is named after one of its major components, known equally the "clathrin coat assembly" ( Fig. 7.four). Information technology consists of clathrin and other proteins such every bit dynamin, adapter proteins and multiple unknown proteins (claimed to exist xl) that together aids in the uptake of receptor-bound complex (Foroozandeh and Aziz, 2018). This process is initiated later the bounden of the ligand with the receptor molecule. Receptors tin either be present on the surface or highly concentrated in pits (transferrin receptors). It is observed that the receptors which are non concentrated in coated pits accept more time to get internalized (Nichols and Lippincott-Schwartz, 2001). Then the receptor–ligand complex will lengthened laterally in search of the coated pits that occupy 1.0%–ii.0% of the total surface area of the plasma membrane.

Figure 7.4. Description of receptor-mediated endocytosis. The process commences later on the attaching of ligands with receptors that are expressed at the outer surface of the plasma membrane or these tin can also be nowadays in an internalized fashion depending upon the blazon of jail cell. The first step represents the germination of the receptor–ligand complex. The 2d step shows the lateral diffusion of the receptor–ligand complex in search of the coated pit which will finally internalize the complex. The third pace represents the formation of a complete endosome mediated by various components such as dynamin, clathrin, and adaptin. Further steps exhibit the process of uncoating of the vesicle so that it should exist able to fuse to form an early endosome. The final footstep decides the fate of the internalized content which can either be degraded after fusion by lysosome or can be recycled back to the trans-Golgi network. Another pathway is transcytosis, which returns the content to the other side of the cellular membrane.

Various plasma membrane proteins, such equally clathrin, dynamin, and adapter protein, are transported to the coated pits, where they assemble in a specific manner and aid in the germination of membrane invagination. Clathrin, attributable to its triskelion structure, can arrange itself either in hexagonal or pentagonal assembly resulting in a driving strength to induce the formation of a vesicle from a flat membrane surface surface area. Adapter proteins also assist in constituting the assembly of clathrin glaze and the process is GTP dependent. Dynamin, on the other hand, helps in pinching off the membrane invagination (Raiborg et al., 2002).

After the internalization of the vesicle, uncoating occurs where the clathrin coat is removed and all the proteins constituting the assembly return to their respective positions on the plasma membrane (Fig. 7.5). Removal of glaze involves several proteins, such as auxillin, heat daze proteins, and synaptojanin. Uncoating is necessary to enable the fusion with trans-Golgi network proteins to grade early endosomes. Again, the fusion procedure as well involves several components among which early on endosomal autoantigen as well serves as a mark. Meanwhile, rab5 too assists in the fusion and helps in the move of early endosome. Besides, the formed receptor–ligand complex then dissociates, which leads to the recycling of receptors followed by the formation of early on endosomes (Piper and Luzio, 2001). Then the germination of late endosome takes identify, mechanisms that are still unknown. There tin can be 3 possibilities with the internalized cargo molecules (Gruenberg and Maxfield, 1995). The first possibility is that the cargo molecules are carried to the lysosome for degradation. In the second probability, the cargo molecules can be recycled back to the trans-Golgi network. Another option involves transcytosis where the molecules are transported on the other side of the membrane (Thomsen et al., 2002).

Figure vii.5. Clathrin-dependent endocytosis showing rapidly uncoating of vesicles.

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