COPI is a coatomer, a protein complex [1] that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments.

Nov 27, 2023 · To discover senolytic targets, we performed RNAi screens and identified coatomer complex I (COPI) vesicle formation as a liability of senescent cells.

Oct 1, 2011 · This review describes the COPII and COPI coating machineries that generate carrier vesicles and the tethers and SNAREs that mediate COPII and COPI vesicle fusion at the ER-Golgi interface.

Dec 13, 2022 · COPI-coated vesicles mediate transport between Golgi stacks and retrograde transport from the Golgi to the endoplasmic reticulum. The COPI coat exists as a stable heptameric complex in the cytosol termed coatomer and is recruited en bloc to the membrane for vesicle formation.

Mar 18, 2009 · Coat protein II (COPII; green) forms vesicles for anterograde transport from the endoplasmic reticulum (ER) to the Golgi, whereas COPI (red) forms vesicles for both intra-Golgi transport and ...

COPI-coated vesicles mediate trafficking within the Golgi apparatus and from the Golgi to the endoplasmic reticulum. The structures of membrane protein coats, including COPI, have been extensively studied with in vitro reconstitution systems using purified components.

Coat Protein I (COPI) is one of the most intensely investigated coat complexes. Numerous studies have contributed to a general understanding of how coat proteins act to initiate intracellular vesicular transport. This review highlights key recent findings that have shaped our current understanding of how COPI vesicles are formed.

Mar 13, 2018 · In this Cell Science at a Glance and accompanying poster, we illustrate the different stages of COPI-coated vesicle formation and revisit decades of research in the context of recent advances in the elucidation of COPI coat structure.

Jul 10, 2015 · Dodonova et al. applied cryo–electron tomography to determine the structure of the COPI coat in its fully assembled form on budded vesicles (see the Perspective by Noble and Stagg). They combined structural data with cross-linking mass spectrometry to generate a complete molecular model.

Here, we summarize current knowledge of COPI coat protein structure; we describe how structural and biochemical studies contributed to this knowledge; we review mechanistic insights into COPI vesicle biogenesis and disassembly; and we discuss the potential to answer open questions in the field.