Linking endocytic cargo to clathrin: structural and functional insights into coated vesicle formation.

  title={Linking endocytic cargo to clathrin: structural and functional insights into coated vesicle formation.},
  author={David. J. Owen},
  journal={Biochemical Society transactions},
  volume={32 Pt 1},
  • D. Owen
  • Published 1 February 2004
  • Biology, Chemistry
  • Biochemical Society transactions
Clathrin-mediated endocytosis is the major process by which transmembrane proteins are internalized from the cell's limiting membrane into the first compartment of the endosomal system, the early endosome. From here, these transmembrane cargo proteins, which are of widely varying type and function, are trafficked to their required destination. Endocytosis plays, therefore, an important role in cell signalling, nutrient uptake, cellular homoeostasis and the interaction of the cell with its… 

Clathrin-mediated transport: assembly required. Workshop on Molecular Mechanisms of Vesicle Selectivity.

This workshop focused on the mechanisms that mediate the formation of transport intermediaries, which carry cargo between intracellular compartments and the plasma membrane, which are the best characterized and are therefore often considered a model for transport-intermediary formation.

Clathrin Adaptor Proteins in Cargo Endocytosis

Evidence suggests that the clathrin coat utilizes a diverse collection ofClathrin-associated sorting proteins (CLASPs) to ensure the efficient and noncompetitive concentration of a wide variety of sorting signals within transport vesicles forming at the cell surface.

Clathrin and Clathrin-Adaptors

An Extended Tyrosine‐Targeting Motif for Endocytosis and Recycling of the Dense‐Core Vesicle Membrane Protein Phogrin

An independent DCV targeting motif in the cytosolic domain that may function at the level of endocytosis and recycling is described.

The Endocytic Pathway

The main mechanisms of internalization are summarized, the endocytic compartments and the pathways that connect them are described, and the processes that direct sorting along these different pathways are examined.

Using quantum dots to visualize clathrin associations

The images obtained with quantum dot technology allow accurate and specific localization of clathrin and theClathrin adaptor protein, AP-2, with cellular organelles and suggest that some of the structures classified as typical coated vesicles by immunocytochemical light microscopic techniques actually may be membrane bound pits.

Recognition of basic sorting motifs within synaptic membrane cargo proteins by the clathrin-adaptor complex AP-2

Recognition of the dibasic sorting motif by µ2-adaptin provides a direct link to the endocytic machinery, and is thereby involved in CME of excitatory AMPA type glutamate receptors similar to the recognition of the SVP synaptotagmin 1 by AP-2.

Inhibition of endocytic pathways impacts cytomegalovirus maturation

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The endophilin–CIN85–Cbl complex mediates ligand-dependent downregulation of c-Met

Inhibition of complex formation is sufficient to block HGF receptor internalization and to enhance HGF-induced signal transduction and biological responses, and disclose a novel functional role for Cbl in HGF receptors signalling.

Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains

The structures of the VHS domain of human GGA3 complexed with signals from both mannose-6-phosphate receptors are reported, highlighting an Asp residue separated by two residues from a dileucine sequence as critical recognition elements.

Curvature of clathrin-coated pits driven by epsin

It is shown here that epsin 1 directly modifies membrane curvature on binding to PtdIns(4,5)P2 in conjunction with clathrin polymerization, and it is proposed that this helix is inserted into one leaflet of the lipid bilayer, inducing curvature.

Nature (London) 419

  • 2002

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  • 2000