COPI acts in both vesicular and tubular transport

Author:  ["Jia-Shu Yang","Carmen Valente","Roman S. Polishchuk","Gabriele Turacchio","Emilie Layre","D. Branch Moody","Christina C. Leslie","Michael H. Gelb","William J. Brown","Daniela Corda","Alberto Luini","Victor W. Hsu"]

Publication:  Nature Cell Biology

CITE.CC academic search helps you expand the influence of your papers.

Tags:  631   80%26kwrd%3DMembrane trafficking   Biological

Abstract

Hsu and colleagues show that COPI-coated buds are a common progenitor for both vesicles and tubules. The choice between these two carriers is mediated by the opposing activities of the acyltransferase LPAAT-γ and the phospholipase cPLA2-α. Intracellular transport occurs through two general types of carrier, either vesicles1,2 or tubules3,4. Coat proteins act as the core machinery that initiates vesicle formation1,2, but the counterpart that initiates tubule formation has been unclear. Here, we find that the coat protein I (COPI) complex initially drives the formation of Golgi buds. Subsequently, a set of opposing lipid enzymatic activities determines whether these buds become vesicles or tubules. Lysophosphatidic acid acyltransferase-γ (LPAATγ) promotes COPI vesicle fission for retrograde vesicular transport. In contrast, cytosolic phospholipase A2-α (cPLA2α) inhibits this fission event to induce COPI tubules, which act in anterograde intra-Golgi transport and Golgi ribbon formation. These findings not only advance a molecular understanding of how COPI vesicle fission is achieved, but also provide insight into how COPI acts in intra-Golgi transport and reveal an unexpected mechanistic relationship between vesicular and tubular transport.

Cite this article

Yang, JS., Valente, C., Polishchuk, R. et al. COPI acts in both vesicular and tubular transport. Nat Cell Biol 13, 996–1003 (2011). https://doi.org/10.1038/ncb2273

View full text

>> Full Text:   COPI acts in both vesicular and tubular transport

Mir193b–365 is essential for brown fat differentiation

A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless