Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane

Clathrin-mediated vesicular trafficking events underpin the vectorial transfer of macromolecules between several eukaryotic membrane-bound compartments. Classical models for coat operation, focused principally on interactions between clathrin, the heterotetrameric adaptor complexes, and cargo molecu...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2005-07, Vol.1744 (3), p.415-437
Main Author: Traub, Linton M.
Format: Article
Language:English
Subjects:
Adaptor Proteins, Vesicular Transport - chemistry
Adaptor Proteins, Vesicular Transport - metabolism
Amino Acid Sequence
Animals
AP-1/AP-2 adaptors
Cargo selection
Cell Membrane - metabolism
Clathrin - chemistry
Clathrin - metabolism
Clathrin-coated vesicle
Molecular Sequence Data
Phosphoinositide
Phosphorylation
Protein Conformation
Protein Transport
Receptor sorting
trans-Golgi Network - metabolism
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Summary:Clathrin-mediated vesicular trafficking events underpin the vectorial transfer of macromolecules between several eukaryotic membrane-bound compartments. Classical models for coat operation, focused principally on interactions between clathrin, the heterotetrameric adaptor complexes, and cargo molecules, fail to account for the full complexity of the coat assembly and sorting process. New data reveal that targeting of clathrin adaptor complexes is generally supported by phosphoinositides, that cargo recognition by heterotetrameric adaptors depends on phosphorylation-driven conformational alterations, and that dedicated clathrin-associated sorting proteins (CLASPs) exist to promote the selective trafficking of specific categories of cargo. A host of accessory factors also participate in coat polymerization events, and the independently folded appendage domains that project off the heterotetrameric adaptor core function as recruitment platforms that appear to oversee assembly operations. It is also now clear that focal polymerization of branched actin microfilaments contributes to clathrin-coated vesicle assembly and movement at both plasma membrane and Golgi sites. This improved appreciation of the complex mechanisms governing clathrin-dependent sorting events reveals several common principles of clathrin operation at the Golgi and the plasma membrane.
ISSN:0167-4889
0006-3002
1879-2596
DOI:10.1016/j.bbamcr.2005.04.005