Literature DB >> 23996193

Components of the CtBP1/BARS-dependent fission machinery.

Carmen Valente1, Alberto Luini, Daniela Corda.   

Abstract

The brefeldin A ADP-ribosylated substrate, a member of the C-terminal-binding protein family that is referred to as CtBP1/BARS, is a dual-function protein that acts as a transcriptional co-repressor in the nucleus and as an inducer of membrane fission in the cytoplasm. In this review, we first discuss the mechanisms that enable CtBP1/BARS to shift between the nuclear transcriptional co-repressor and the cytosolic fission-inducing activities. Then, we focus on the role of CtBP1/BARS in membrane fission. CtBP1/BARS controls several fission events including macropinocytosis, fluid-phase endocytosis, COPI-coated vesicle formation, basolaterally directed post-Golgi carrier formation, and Golgi partitioning in mitosis. We report on recent advances in our understanding of the CtBP1/BARS membrane fission machineries that operate at the trans-side and at the cis-side of the Golgi complex. Specifically, we discuss how these machineries are assembled and regulated, and how they operate in the formation of the basolaterally directed post-Golgi carriers.

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Year:  2013        PMID: 23996193     DOI: 10.1007/s00418-013-1138-1

Source DB:  PubMed          Journal:  Histochem Cell Biol        ISSN: 0948-6143            Impact factor:   4.304


  133 in total

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6.  The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS.

Authors:  Prisca Liberali; Elina Kakkonen; Gabriele Turacchio; Carmen Valente; Alexander Spaar; Giuseppe Perinetti; Rainer A Böckmann; Daniela Corda; Antonino Colanzi; Varpu Marjomaki; Alberto Luini
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10.  CtBP1/BARS is an activator of phospholipase D1 necessary for agonist-induced macropinocytosis.

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7.  Golgi membrane fission requires the CtBP1-S/BARS-induced activation of lysophosphatidic acid acyltransferase δ.

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