Mechanisms of vesicle formation: Insights from the COP system

https://doi.org/10.1016/S0955-0674(99)80063-5Get rights and content

The major cytosolic and membrane proteins that represent machinery of coat protein (COP)-coated transport vesicles within the secretory pathway are characterized to date. This has allowed investigation of the molecular mechanisms that underlie the formation of these vesicles. In vitro binding studies and reconstitution experiments have provided insights at the molecular level into the biogenesis of COPII- and COPI-coated vesicles.

References and recommended reading (54)

  • MatsuokaK et al.

    Coat assembly directs v-SNARE concentration into synthetic COPII vesicles

    Mol Cell

    (1998)
  • BremserM et al.

    Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors

    Cell

    (1999)
  • MatsuokaK et al.

    COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes

    Cell

    (1998)
  • HarterC et al.

    A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer

  • PalmerDJ et al.

    Binding of coatomer to Golgi membranes requires AOP-ribosylation factor

    J Biol Chem

    (1993)
  • BrownMT et al.

    ASAP1, a phospholipid-dependent ARF GTPase-activating protein that associates with and is phosphorylated by Src

    Mol Cell Biol

    (1998)
  • RothmanJE et al.

    Protein sorting by transport vesicles

    Science

    (1996)
  • SchekmanR et al.

    Coat proteins and vesicle budding

    Science

    (1996)
  • LeBorgne R et al.

    Mechanisms of protein sorting and coat assembly: insights from the clathrin-coated vesicle pathway

    Curr Opin Cell Biol

    (1998)
  • BarloweC et al.

    COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum

    Cell

    (1994)
  • BarloweC et al.

    SEC12 encodes a guanine nucleotide exchange factor essential for transport vesicle formation from the ER

    Nature

    (1993)
  • ChardinP et al.

    A human exchange factor for ARF contains Sec7-and pleckstrin-homology domains

    Nature

    (1996)
  • OrciL et al.

    Budding from Golgi membranes requires the coatomer complex of non-clathrin coat proteins

    Nature

    (1993)
  • ZhaoL et al.

    Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta

  • YoshihisaT et al.

    Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum

    Science

    (1993)
  • CukiermanE et al.

    The ARF1 GTPase activating protein: zinc finger motif and Golgi complex localization

    Science

    (1995)
  • CossonP et al.

    Coatomer interaction with di-lysine endoplasmic reticulum retention motifs

    Science

    (1994)
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