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Article

Assembly, organization, and function of the COPII coat

3 Dec 2007

Abstract excerpt

A full mechanistic understanding of how secretory cargo proteins are exported from the endoplasmic reticulum for passage through the early secretory pathway is essential for us to comprehend how cells are organized, maintain compartment identity, as well as how they selectively secrete proteins and other macromolecules to the extracellular space. This process depends on the function of a multi-subunit complex,...

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Identifiers

PMID: 18060556
DOI: 10.1007/s00418-007-0363-x

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Assembly, organization, and function of the COPII coatPMID 18060556Read ↗

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Coatopathies: Genetic Disorders of Protein CoatsSemantic proximity Read ↗

COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP.Semantic proximity Read ↗

Dynamic Glycosylation Governs the Vertebrate COPII Protein Trafficking PathwaySemantic proximity Read ↗

Consequences of mutations in the genes of the ER export machinery COPII in vertebrates.Semantic proximity Read ↗

The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus.Semantic proximity Read ↗

Inherited hematological disorders due to defects in coat protein (COP)II complex.Semantic proximity Read ↗

Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic.Semantic proximity Read ↗

Non-clathrin-coat protein alpha is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growth.Semantic proximity Read ↗

Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport.Semantic proximity Read ↗

Novel cargo-binding site in the beta and delta subunits of coatomer.Semantic proximity Read ↗

COPI is essential for Golgi cisternal maturation and dynamics.Semantic proximity Read ↗

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