Coat Proteins and Vesicle Budding

  title={Coat Proteins and Vesicle Budding},
  author={Randy Schekman and Lelio Orci},
  pages={1526 - 1533}
The trafficking of proteins within eukaryotic cells is achieved by the capture of cargo and targeting molecules into vesicles that bud from a donor membrane and deliver their contents to a receiving compartment. This process is bidirectional and may involve multiple organelles within a cell. Distinct coat proteins mediate each budding event, serving both to shape the transport vesicle and to select by direct or indirect interaction the desired set of cargo molecules. Secretion, which has been… 

Coats and vesicle budding.

COPII and secretory cargo capture into transport vesicles.

Endocytosis and transcytosis.

  • Okamoto
  • Biology, Chemistry
    Advanced drug delivery reviews
  • 1998

Vesicular transport: the core machinery of COPI recruitment and budding.

This work has generated a model that covers the cycle of coat recruitment, coat polymerization, vesicle budding and uncoating in COPI vesicles, and shed light on the mechanism of COPIvesicle biogenesis.

Bi-directional protein transport between the ER and Golgi.

This work reviews the mechanisms that govern coat recruitment to the membrane, cargo capture into a transport vesicle, and accurate delivery to the target organelle.

Coat proteins: shaping membrane transport

Recent findings indicate that coat proteins might also participate in the differentiation of membrane domains within organelles and large transport carriers, as well as in the association of the carriers with the cytosketelon and with acceptor organlles.

Clathrin-coated vesicle formation and protein sorting: an integrated process.

  • S. Schmid
  • Biology, Chemistry
    Annual review of biochemistry
  • 1997
The functional interplay between the coated vesicle machinery and its cargo could ensure sorting fidelity and packaging efficiency and might enable modulation of vesicular trafficking in response to demand.

Coupling of Coat Assembly and Vesicle Budding to Packaging of Putative Cargo Receptors




Uncoupled Packaging of Targeting and Cargo Molecules during Transport Vesicle Budding from the Endoplasmic Reticulum (*)

It is document that endoplasmic reticulum devoid of cargo proteins is competent in the formation and release of targeting molecule-containing vesicles in a fashion indistinguishable from its normal counterpart.

The role of clathrin, adaptors and dynamin in endocytosis.

  • M. Robinson
  • Biology, Chemistry
    Current opinion in cell biology
  • 1994

An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding.

A role for this protein family in the budding of coatamer-coated and other species of coated vesicles is indicated as well as a role for the p24 isoform in yeast and humans.

Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles.

The vesicles produced are functionally distinct from the ER: they transfer pro-alpha-factor to the Golgi apparatus faster and more efficiently than the ER, they do not require Sec12p or Sec23p to complete transfer, and transfer is resistant to GTP gamma S.

Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol

It is shown that coatomer and ARF are the only cytoplasmic proteins needed for the assembly and budding of COP-coated vesicles and COP- coated buds may form essentially by self-assembly from Golgi cisternae after an initial step in which GTP is used to allow ARF binding.

ADP-ribosylation factor and coatomer couple fusion to vesicle budding

The coat proteins required for budding COP-coated vesicles from Golgi membranes, coatomer and ADP-ribosylation factor (ARF) protein, are shown to be required to reconstitute the orderly process of

Mediation of the attachment or fusion step in vesicular transport by the GTP-binding Ypt1 protein

A specific GTP-binding protein is required for either attachment or fusion (or both) of secretory vesicles with the acceptor compartment during protein secretion.