Academic literature on the topic 'Clathrin-coated pits'

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Journal articles on the topic "Clathrin-coated pits"

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Wu, Xufeng, Xiaohong Zhao, Lauren Baylor, Shivani Kaushal, Evan Eisenberg, and Lois E. Greene. "Clathrin exchange during clathrin-mediated endocytosis." Journal of Cell Biology 155, no. 2 (2001): 291–300. http://dx.doi.org/10.1083/jcb.200104085.

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During clathrin-mediated endocytosis, clathrin-coated pits invaginate to form clathrin-coated vesicles (CVs). Since clathrin-coated pits are planar structures, whereas CVs are spherical, there must be a structural rearrangement of clathrin as invagination occurs. This could occur through simple addition of clathrin triskelions to the edges of growing clathrin-coated pits with very little exchange occurring between clathrin in the pits and free clathrin in the cytosol, or it could occur through large scale exchange of free and bound clathrin. In the present study, we investigated this question by studying clathrin exchange both in vitro and in vivo. We found that in vitro clathrin in CVs and clathrin baskets do not exchange with free clathrin even in the presence of Hsc70 and ATP where partial uncoating occurs. However, surprisingly FRAP studies on clathrin-coated pits labeled with green fluorescent protein–clathrin light chains in HeLa cells show that even when endocytosis is blocked by expression of a dynamin mutant or depletion of cholesterol from the membrane, replacement of photobleached clathrin in coated pits on the membrane occurs at almost the same rate and magnitude as when endocytosis is occurring. Furthermore, very little of this replacement is due to dissolution of old pits and reformation of new ones; rather, it is caused by a rapid ATP-dependent exchange of clathrin in the pits with free clathrin in the cytosol. On the other hand, consistent with the in vitro data both potassium depletion and hypertonic sucrose, which have been reported to transform clathrin-coated pits into clathrin cages just below the surface of the plasma membrane, not only block endocytosis but also block exchange of clathrin. Taken together, these data show that ATP-dependent exchange of free and bound clathrin is a fundamental property of clathrin-coated pits, but not clathrin baskets, and may be involved in a structural rearrangement of clathrin as clathrin-coated pits invaginate.
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Wu, Xufeng, Xiaohong Zhao, Rosa Puertollano, Juan S. Bonifacino, Evan Eisenberg, and Lois E. Greene. "Adaptor and Clathrin Exchange at the Plasma Membrane andtrans-Golgi Network." Molecular Biology of the Cell 14, no. 2 (2003): 516–28. http://dx.doi.org/10.1091/mbc.e02-06-0353.

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We previously demonstrated, using fluorescence recovery after photobleaching, that clathrin in clathrin-coated pits at the plasma membrane exchanges with free clathrin in the cytosol, suggesting that clathrin-coated pits are dynamic structures. We now investigated whether clathrin at the trans-Golgi network as well as the clathrin adaptors AP2 and AP1 in clathrin-coated pits at the plasma membrane and trans-Golgi network, respectively, also exchange with free proteins in the cytosol. We found that when the budding of clathrin-coated vesicle is blocked without significantly affecting the structure of clathrin-coated pits, both clathrin and AP2 at the plasma membrane and clathrin and AP1 at thetrans-Golgi network exchange rapidly with free proteins in the cytosol. In contrast, when budding of clathrin-coated vesicles was blocked at the plasma membrane or trans-Golgi network by hypertonic sucrose or K+ depletion, conditions that markedly affect the structure of clathrin-coated pits, clathrin exchange was blocked but AP2 at the plasma membrane and both AP1 and the GGA1 adaptor at the trans-Golgi network continue to rapidly exchange. We conclude that clathrin-coated pits are dynamic structures with rapid exchange of both clathrin and adaptors and that adaptors are able to exchange independently of clathrin when clathrin exchange is blocked.
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ANDERSON, R. "Dissecting clathrin-coated pits." Trends in Cell Biology 3, no. 6 (1993): 177–79. http://dx.doi.org/10.1016/0962-8924(93)90205-f.

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Zhao, X., T. Greener, H. Al-Hasani, S. W. Cushman, E. Eisenberg, and L. E. Greene. "Expression of auxilin or AP180 inhibits endocytosis by mislocalizing clathrin: evidence for formation of nascent pits containing AP1 or AP2 but not clathrin." Journal of Cell Science 114, no. 2 (2001): 353–65. http://dx.doi.org/10.1242/jcs.114.2.353.

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Although uncoating of clathrin-coated vesicles is a key event in clathrin-mediated endocytosis it is unclear what prevents uncoating of clathrin-coated pits before they pinch off to become clathrin-coated vesicles. We have shown that the J-domain proteins auxilin and GAK are required for uncoating by Hsc70 in vitro. In the present study, we expressed auxilin in cultured cells to determine if this would block endocytosis by causing premature uncoating of clathrin-coated pits. We found that expression of auxilin indeed inhibited endocytosis. However, expression of auxilin with its J-domain mutated so that it no longer interacted with Hsc70 also inhibited endocytosis as did expression of the clathrin-assembly protein, AP180, or its clathrin-binding domain. Accompanying this inhibition, we observed a marked decrease in clathrin associated with the plasma membrane and the trans-Golgi network, which provided us with an opportunity to determine whether the absence of clathrin from clathrin-coated pits affected the distribution of the clathrin assembly proteins AP1 and AP2. Surprisingly we found almost no change in the association of AP2 and AP1 with the plasma membrane and the trans-Golgi network, respectively. This was particularly obvious when auxilin or GAK was expressed with functional J-domains since, in these cases, almost all of the clathrin was sequestered in granules that also contained Hsc70 and auxilin or GAK. We conclude that expression of clathrin-binding proteins inhibits clathrin-mediated endocytosis by sequestering clathrin so that it is no longer available to bind to nascent pits but that assembly proteins bind to these pits independently of clathrin.
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Shen, Hongying, Shawn M. Ferguson, Noah Dephoure, et al. "Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin." Molecular Biology of the Cell 22, no. 4 (2011): 493–502. http://dx.doi.org/10.1091/mbc.e10-07-0637.

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Clathrin-mediated endocytosis is a fundamental cellular process conserved from yeast to mammals and is an important endocytic route for the internalization of many specific cargos, including activated growth factor receptors. Here we examined changes in tyrosine phosphorylation, a representative output of growth factor receptor signaling, in cells in which endocytic clathrin-coated pits are frozen at a deeply invaginated state, that is, cells that lack dynamin (fibroblasts from dynamin 1, dynamin 2 double conditional knockout mice). The major change observed in these cells relative to wild-type cells was an increase in the phosphorylation state, and thus activation, of activated Cdc42-associated kinase (Ack), a nonreceptor tyrosine kinase. Ack is concentrated at clathrin-coated pits, and binds clathrin heavy chain via two clathrin boxes. RNA interference–based approaches and pharmacological manipulations further demonstrated that the phosphorylation of Ack requires both clathrin assembly into endocytic clathrin-coated pits and active Cdc42. These findings reveal a link between progression of clathrin-coated pits to endocytic vesicles and an activation–deactivation cycle of Ack.
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Chen, Yan, Jeffery Yong, Antonio Martínez-Sánchez, et al. "Dynamic instability of clathrin assembly provides proofreading control for endocytosis." Journal of Cell Biology 218, no. 10 (2019): 3200–3211. http://dx.doi.org/10.1083/jcb.201804136.

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Clathrin-mediated endocytosis depends on the formation of functional clathrin-coated pits that recruit cargos and mediate the uptake of those cargos into the cell. However, it remains unclear whether the cargos in the growing clathrin-coated pits are actively monitored by the coat assembly machinery. Using a cell-free reconstitution system, we report that clathrin coat formation and cargo sorting can be uncoupled, indicating that a checkpoint is required for functional cargo incorporation. We demonstrate that the ATPase Hsc70 and a dynamic exchange of clathrin during assembly are required for this checkpoint. In the absence of Hsc70 function, clathrin assembles into pits but fails to enrich cargo. Using single-molecule imaging, we further show that uncoating takes place throughout the lifetime of the growing clathrin-coated pits. Our results suggest that the dynamic exchange of clathrin, at the cost of the reduced overall assembly rates, primarily serves as a proofreading mechanism for quality control of endocytosis.
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Johannessen, Lene E., Nina Marie Pedersen, Ketil Winther Pedersen, Inger Helene Madshus, and Espen Stang. "Activation of the Epidermal Growth Factor (EGF) Receptor Induces Formation of EGF Receptor- and Grb2-Containing Clathrin-Coated Pits." Molecular and Cellular Biology 26, no. 2 (2006): 389–401. http://dx.doi.org/10.1128/mcb.26.2.389-401.2006.

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ABSTRACT In HeLa cells depleted of adaptor protein 2 complex (AP2) by small interfering RNA (siRNA) to the μ2 or α subunit or by transient overexpression of an AP2 sequestering mutant of Eps15, endocytosis of the transferrin receptor (TfR) was strongly inhibited. However, epidermal growth factor (EGF)-induced endocytosis of the EGF receptor (EGFR) was inhibited only in cells where the α subunit had been knocked down. By immunoelectron microscopy, we found that in AP2-depleted cells, the number of clathrin-coated pits was strongly reduced. When such cells were incubated with EGF, new coated pits were formed. These contained EGF, EGFR, clathrin, and Grb2 but not the TfR. The induced coated pits contained the α subunit, but labeling density was reduced compared to control cells. Induction of clathrin-coated pits required EGFR kinase activity. Overexpression of Grb2 with inactivating point mutations in N- or C-terminal SH3 domains or in both SH3 domains inhibited EGF-induced formation of coated pits efficiently, even though Grb2 SH3 mutations did not block activation of mitogen-activated protein kinase (MAPK) or phosphatidylinositol 3-kinase (PI3K). Our data demonstrate that EGFR-induced signaling and Grb2 are essential for formation of clathrin-coated pits accommodating the EGFR, while activation of MAPK and PI3K is not required.
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Santini, F., and J. H. Keen. "Endocytosis of activated receptors and clathrin-coated pit formation: deciphering the chicken or egg relationship." Journal of Cell Biology 132, no. 6 (1996): 1025–36. http://dx.doi.org/10.1083/jcb.132.6.1025.

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The fundamental mechanisms by which receptors once targeted for endocytosis are found in coated pits is an important yet unresolved question. Specifically, are activated receptors simply trapped on encountering preexisting coated pits, subsequently being rapidly internalized? Or do the receptors themselves, by active recruitment, gather soluble coat and cytosolic components and initiate the rapid assembly of new coated pits that then mediate their internalization? To explore this question, we studied the relationship between activation of IgE-bound high affinity Fc receptors (FCepsilonRI) and coated pit formation. Because these receptors are rapidly internalized via clathrin-coated pits only when cross-linked by the binding of multivalent antigens, we were able to separate activation from internalization by using an immobilized antigen. The FCepsilonRIs, initially uniformly distributed over the cell surface. relocalized and aggregated on the antigen-exposed membrane. The process was specific for the antigen, and temperature- and time-dependent. This stimulation initiated a cascade of cellular responses typical of FCepsilonRI signaling including membrane ruffling, cytoskeletal rearrangements, and, in the presence of Ca2+, exocytosis. Despite these responses, no change in coated pit disposition or in the distribution of clathrin and assembly protein AP2 was detected, as monitored by immunoblotting and by quantitative (vertical sectioning) confocal microscopy analysis of immunofluorescently stained cells. Specifically, there was no decrease in the density of clathrin-coated pits in regions of the cell membrane not in contact with the antigen, and there was no apparent increase in clathrin-coated pits in proximity to stimulated FCepsilonRI receptors as would have been expected if the receptors were inducing formation of new pits by active recruitment. These results indicate that de novo formation of clathrin-coated pits is not a prerequisite for rapid internalization or a direct response to stimulation of FCepsilonRI receptors. Therefore, increases in coated pits reported to occur in response to activation of some signaling receptors must be consequences of the signal transduction processes, rather than strictly serving the purpose of the internalization of the receptors.
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Rappoport, Joshua, Sanford M. Simon, and Alexandre Benmerah. "Understanding Living Clathrin-Coated Pits." Traffic 5, no. 5 (2004): 327–37. http://dx.doi.org/10.1111/j.1398-9219.2004.00187.x.

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Hansen, S. H., K. Sandvig, and B. van Deurs. "Clathrin and HA2 adaptors: effects of potassium depletion, hypertonic medium, and cytosol acidification." Journal of Cell Biology 121, no. 1 (1993): 61–72. http://dx.doi.org/10.1083/jcb.121.1.61.

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The effects of methods known to perturb endocytosis from clathrin-coated pits on the localization of clathrin and HA2 adaptors in HEp-2 carcinoma cells have been studied by immunofluorescence and ultrastructural immunogold microscopy, using internalization of transferrin as a functional assay. Potassium depletion, as well as incubation in hypertonic medium, remove membrane-associated clathrin lattices: flat clathrin lattices and coated pits from the plasma membrane, and clathrin-coated vesicles from the cytoplasm, as well as those budding from the TGN. In contrast, immunofluorescence microscopy using antibodies specific for the alpha- and beta-adaptins, respectively, and immunogold labeling of cryosections with anti-alpha-adaptin antibodies shows that under these conditions HA2 adaptors are aggregated at the plasma membrane to the same extent as in control cells. After reconstitution with isotonic K(+)-containing medium, adaptor aggregates and clathrin lattices colocalize at the plasma membrane as normally and internalization of transferrin resumes. Acidification of the cytosol affects neither clathrin nor HA2 adaptors as studied by immunofluorescence microscopy. However, quantitative ultrastructural observations reveal that acidification of the cytosol results in formation of heterogeneously sized and in average smaller clathrin-coated pits at the plasma membrane and buds on the TGN. Collectively, our observations indicate that the methods to perturb formation of clathrin-coated vesicles act by different mechanisms: acidification of the cytosol by affecting clathrin-coated membrane domains in a way that interferes with budding of clathrin-coated vesicles from the plasma membrane as well as from the TGN; potassium depletion and incubation in hypertonic medium by preventing clathrin and adaptors from interacting. Furthermore our observations show that adaptor aggregates can exist at the plasma membrane independent of clathrin lattices and raise the possibility that adaptor aggregates can form nucleation sites for clathrin lattices.
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Dissertations / Theses on the topic "Clathrin-coated pits"

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Sowerby, Penelope Jane. "Proteins involved in clathrin coated pit formation at the trans-Golgi network." Thesis, University of Cambridge, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.625022.

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Book chapters on the topic "Clathrin-coated pits"

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Thieman, James R., and Linton M. Traub. "Clathrin-Coated Pits." In Cellular Domains. John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118015759.ch2.

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Liang, Liang, Hongying Shen, Pietro De Camilli, and James S. Duncan. "Tracking Clathrin Coated Pits with a Multiple Hypothesis Based Method." In Medical Image Computing and Computer-Assisted Intervention – MICCAI 2010. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-15745-5_39.

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Kirchhausen, T. "Clathrin-associated protein complexes (APs)." In Secretory Pathway. Oxford University PressOxford, 1994. http://dx.doi.org/10.1093/oso/9780198599425.003.0178.

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Abstract = - - = Clathrin-associated proteins are also referred to as assem bly proteins and adaptors. The term “associated proteins” is a general term used to indicate that their in vivo function is still not completely understood. “Assembly proteins” refers to the in vitro property that under physiological ionic conditions APs interact with clathrin and assemble with it into small coats1 The term “adaptor”2 was introduced to indicate that a possible role of the APs is to interact with clathrin and with the cytoplasmic tails of some membrane proteins, leading to their selection and concentration into coated pits and coated vesicles2,3.
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Chastel, Julia, and Annie Angers. "Recent Advances in the Importance of Ubiquitylation for Receptor Internalization and Signaling." In Physiology. IntechOpen, 2024. http://dx.doi.org/10.5772/intechopen.114990.

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Receptor tyrosine kinases are activated by binding to their ligands, which trigger modifications in their cytoplasmic domains to initiate signal transduction. Control mechanisms to modulate the signaling of growth factor receptors are essential for proper signaling and require several levels of regulation. Post-translational modifications play crucial roles in intracellular trafficking through mechanisms that are not fully understood. Ubiquitylation is recognized as an essential signal in establishing molecular networks controlling receptor internalization and trafficking at the membrane and in sorting endosomes. In turn, receptor trafficking influences how the signaling networks are activated. Recent advances show how receptor targeting to clathrin-coated pits and internalization influences signaling by allowing specific target activation. At the same time, progress has been made in showing how membrane proteins are organized to facilitate the recruitment of activated receptors to clathrin-coated pits and how this whole process depends on the ubiquitylation of the receptors and endocytosis accessory proteins. Here, we review recent advances in the role of ubiquitylation in receptor internalization and trafficking.
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Nagano, Makoto, Junko Y. Toshima, and Jiro Toshima. "Membrane shaping for clathrin-coated pits and endocytosis." In Plasma Membrane Shaping. Elsevier, 2023. http://dx.doi.org/10.1016/b978-0-323-89911-6.00009-1.

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Gjøen, Tor, Trond Olav Berg, and Trond Berg. "Lysosomes and endocytosis." In Subcellular Fractionation. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780199634958.003.0006.

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Abstract Endocytosis is a multistep process whereby molecules are internalized into cells and subsequently transported to one of four destinations: lysosomes, the opposite side of the (epithelial) cell, storage granules, or back to the plasma membrane from which internalization took place. The various steps in the endocytic process are mediated by specialized organelles. Internalization may take place inside or outside coated pits and therefore involves two different areas of the plasma membrane (1). Clathrin-dependent internalization is a well-known process whereas the structure of the plasma membrane that mediates clathrin-independent internalization is not known. Invagination of coated pits leads to coated vesicles from which ‘primary endosomes’ are formed. Clathrin-independent endocytosis leads directly to formation of smooth-surfaced primary endosomes. Primary endosomes carry their cargo to early endosomes that consist of tubules and luminal parts. In some cells the early endosomes may gradually develop into multivesicular bodies. This ‘maturation’ involves formation of internal vesicles and loss of tubular extensions (2). The early endosomes serve as a sorting station. Some endocytic receptors are returned to the plasma membrane in ‘receptosomes’ whereas others follow a transcytotic route to the opposite side of the cells. Some receptors follow the ligand to the lysosomes. In other cells the transport from early to late endosomes may not primarily be due to a maturation process. Instead, specific carrier vesicles may bud off from early endosomes and these are subsequently moved along microtubules to late endosomes (3). The mechanism whereby receptor-ligand complexes are transported from endosomes to lysosomes is not known. Moreover, lysosomes may exist in different states of activity, and functions previously ascribed to lysosomes (e.g. proteolysis), may certainly also take place in endosomes (4). In some cells, such as macrophages, the dense lysosomes may primarily serve as storage granules while the main degradation takes place in a prelysosomal, late endosomal compartment. Transport to lysosomes may be mediated by vesicles budding off from the prelysosomal compartment. In other cells, late endosomes may fuse with lysosomes.
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Gruenberg, Jean, and Jean-Pierre Gorvel. "In vitro reconstitution of endocytic vesicle fusion." In Protein Targeting. Oxford University PressOxford, 1992. http://dx.doi.org/10.1093/oso/9780199632060.003.0008.

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Abstract It is now well established that, after internalization by clathrin-coated pits, solutes and receptors first appear in early endosomes at the cell periphery, then in late endosomes in the perinuclear region, and eventually in lysosomes (reviews in references 1-3). We have observed that tracers leaving the early endosomes appear in large spherical vesicles before they reach late endosomes (4). These large vesicles resemble one of the subpopulations of multivesicular endosomes described by Dunn et al. (5). Tracers internalized after microtubule depolymerization pass through early endosomes and reach these large vesicles but they do not appear in the late endosomes. We thus proposed that these vesicles are involved in the microtubule-dependent transport between early and late endosomes and may correspond to the vesicles observed to move in vivo between the cell periphery and the perinuclear region. In this chapter we will refer to these vesicles as endosomal carrier vesicles.
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Conference papers on the topic "Clathrin-coated pits"

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Kumar, G. Aditya, and Manoj A. Puthenveedu. "GPCR cargo modifies lipid order in clathrin-coated pits." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.158190.

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