Results 191 to 200 of about 85,659 (234)

ARFRP1 functions upstream of ARL1 and ARL5 to coordinate recruitment of distinct tethering factors to the trans-Golgi network. [PDF]

J Cell Biol, 2019
Ishida M, Bonifacino JS.
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Retrograde transport from endosomes to the trans-Golgi network

Nature Reviews Molecular Cell Biology, 2006
A subset of intracellular transmembrane proteins such as acid-hydrolase receptors, processing peptidases and SNAREs, as well as extracellular protein toxins such as Shiga toxin and ricin, undergoes 'retrograde' transport from endosomes to the trans-Golgi network. Here, we discuss recent studies that have begun to unravel the molecular machinery that is
Juan S, Bonifacino, Raul, Rojas
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Rab22B’s role in trans-Golgi network membrane dynamics

Biochemical and Biophysical Research Communications, 2007
The small GTPase Rab22B (or Rab31) has been suspected to be involved in trafficking at trans-Golgi network. However, its exact cellular localization, tissue expression profile, and functions have not been uncharacterized. Specific antibody raised against Rab22B's protein revealed that Rab22B is brain-enriched, but is also present in substantial levels ...
Ng, E.L., Wang, Y., Tang, B.L.
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Secretory cargo sorting at the trans-Golgi network

Trends in Cell Biology, 2014
Sorting of proteins for secretion from cells is crucial for normal physiology and the regulation of key cellular events. Although the sorting of lysosomal hydrolases at the trans-Golgi network (TGN) for delivery to pre-lysosomes is well characterized, the corresponding mechanism by which secreted proteins are sorted for plasma-membrane delivery remains
Kienzle, C., von Blume, J.
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Quantification of Protein Exit at the Trans-Golgi Network

2022
With one-third of all newly synthesized proteins entering the secretory pathway, correct protein sorting is essential for cellular homeostasis. In the last three decades, researchers have developed numerous biochemical, genetic, and cell biological approaches to study protein export and sorting from the trans-Golgi network (TGN).
Mai Ly, Tran, Yeongho, Kim, Julia, von Blume   +2 more
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Phosphoinositides and membrane traffic at the trans-Golgi network.

Biochemical Society Symposia, 2005
Cargo proteins moving along the secretory pathway are sorted at the TGN (trans-Golgi network) into distinct carriers for delivery to the plasma membrane or endosomes. Recent studies in yeast and mammals have shown that formation of these carriers is regulated by PtdIns(4)P.
Choudhury, Rawshan R., Hyvola, Noora, Lowe, Martin   +2 more
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The trans-Golgi network: a late secretory sorting station

Current Opinion in Cell Biology, 1997
Proteins synthesized on membrane-bound ribosomes are transported through the Golgi apparatus and, on reaching the trans-Golgi network, are sorted for delivery to various cellular destinations. Sorting involves the assembly of cytosol-oriented coat structures which preferentially package cargo into vesicular transport intermediates.
L M, Traub, S, Kornfeld
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Multimeric connexin interactions prior to the trans-Golgi network

Journal of Cell Science, 2001
Cells that express multiple connexins have the capacity to form heteromeric (mixed) gap junction hemichannels. We used a dominant negative connexin construct, consisting of bacterial β-galactosidase fused to the C terminus of connexin43 (Cx43/β-gal), to examine connexin compatibility in NIH 3T3 cells. Cx43/β-gal is retained in a perinuclear compartment
J, Das Sarma, R A, Meyer, F, Wang, V, Abraham, C W, Lo, M, Koval   +5 more
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Lipid-dependent protein sorting at the trans-Golgi network

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2012
In eukaryotic cells, the trans-Golgi network serves as a sorting station for post-Golgi traffic. In addition to coat- and adaptor-mediated mechanisms, studies in mammalian epithelial cells and yeast have provided evidence for lipid-dependent protein sorting as a major delivery mechanism for cargo sorting to the cell surface.
Surma, M., Klose, C., Simons, K.
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Trans-Golgi network breaks away to activate NLRP3

Nature Reviews Immunology, 2019
NLRP3 activators cause disassembly of the trans-Golgi network, and the dispersed trans-Golgi network serves as a scaffold for NLRP3 inflammasome assembly and activation.
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