Results 211 to 220 of about 63,639 (257)
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Annual Review of Biochemistry, 2000
▪ Abstract Clathrin was discovered nearly 25 years ago. Since then, a large number of other proteins that participate in the process by which clathrin-coated vesicles retrieve synaptic membranes or take up endocytic receptors have been identified. The functional relationships among these disparate components remain, in many cases, obscure.
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▪ Abstract Clathrin was discovered nearly 25 years ago. Since then, a large number of other proteins that participate in the process by which clathrin-coated vesicles retrieve synaptic membranes or take up endocytic receptors have been identified. The functional relationships among these disparate components remain, in many cases, obscure.
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Clathrin- and non-clathrin-coated vesicle adaptors
Trends in Biochemical Sciences, 1991Recent advances in our understanding of the protein components of the coat of non-clathrin-coated vesicles has revealed the similarity between one component of the non-clathrin coat and the adaptor proteins of clathrin-coated vesicles. This non-clathrin coat adaptor (β-COP) appears to be directly affected by Brefeldin A, a drug which inhibits secretion,
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Trends in Cell Biology, 1994
Internalization of membrane, fluid and receptor-bound ligands into cells occurs by at least two endocytic mechanisms. One is dependent on clathrin and responsible for concentrative uptake of growth factors and other ligands, whereas the other operates without clathrin.
Sandvig, Kirsten, van Deurs, Bo
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Internalization of membrane, fluid and receptor-bound ligands into cells occurs by at least two endocytic mechanisms. One is dependent on clathrin and responsible for concentrative uptake of growth factors and other ligands, whereas the other operates without clathrin.
Sandvig, Kirsten, van Deurs, Bo
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Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
Nature Reviews Molecular Cell Biology, 2005The internalization of various cargo proteins and lipids from the mammalian cell surface occurs through the clathrin and lipid-raft endocytic pathways. Protein-lipid and protein-protein interactions control the targeting of signalling molecules and their partners to various specialized membrane compartments in these pathways.
Christine Le Roy
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Endocytosis without clathrin coats
Trends in Cell Biology, 2001Endocytosis is involved in an enormous variety of cellular processes. To date, most studies on endocytosis in mammalian cells have focused on pathways that start with uptake through clathrin-coated pits. Recently, new techniques and reagents have allowed a wider range of endocytic pathways to begin to be characterized.
B J, Nichols, J, Lippincott-Schwartz
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1999
Abstract Clathrin is a triskelion-shaped, self-assembling protein which polymerizes into a polyhedral lattice on the cytoplasmic surface of cellular membranes. Formation of the clathrin lattice constitutes a mechanism for sorting membrane-associated proteins which are incorporated into the lattice via bridging proteins, known as adaptors
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Abstract Clathrin is a triskelion-shaped, self-assembling protein which polymerizes into a polyhedral lattice on the cytoplasmic surface of cellular membranes. Formation of the clathrin lattice constitutes a mechanism for sorting membrane-associated proteins which are incorporated into the lattice via bridging proteins, known as adaptors
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Nature Cell Biology, 2012
Clathrin adaptor proteins are essential for clathrin-coated vesicle biogenesis, yet the mechanisms governing their recruitment and interactions remain incompletely defined. The clathrin adaptors Gga and AP-1 are now shown to be recruited sequentially to the trans-Golgi network in two waves of clathrin coat assembly, coupled by Pik1-mediated ...
Yidi, Sun, David G, Drubin
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Clathrin adaptor proteins are essential for clathrin-coated vesicle biogenesis, yet the mechanisms governing their recruitment and interactions remain incompletely defined. The clathrin adaptors Gga and AP-1 are now shown to be recruited sequentially to the trans-Golgi network in two waves of clathrin coat assembly, coupled by Pik1-mediated ...
Yidi, Sun, David G, Drubin
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American Journal of Physiology-Cell Physiology, 2000
Subconfluent cultures of Madin-Darby canine kidney (MDCK) and CV-1 cells were immunostained with two monoclonal antibodies (MAbs), MAb X-22 and MAb 23, against clathrin heavy chain and with polyclonal antiserum against a conserved region of all mammalian clathrin light chains.
C T, Okamoto, J, McKinney, Y Y, Jeng
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Subconfluent cultures of Madin-Darby canine kidney (MDCK) and CV-1 cells were immunostained with two monoclonal antibodies (MAbs), MAb X-22 and MAb 23, against clathrin heavy chain and with polyclonal antiserum against a conserved region of all mammalian clathrin light chains.
C T, Okamoto, J, McKinney, Y Y, Jeng
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