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| Subject Categories: Membranes & Transport | Microbiology & Pathogens |
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| The EMBO Journal
(2008) 27, 970–981, doi:10.1038/emboj.2008.59 Published online 20 March 2008 |
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| The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS |
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| Prisca Liberali1, Elina Kakkonen2, Gabriele Turacchio3, Carmen Valente1, Alexander Spaar3, Giuseppe Perinetti1, Rainer A Böckmann4, Daniela Corda1, Antonino Colanzi1, Varpu Marjomaki2 and Alberto Luini3 |
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1 Laboratory of Cell Regulation, Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Santa Maria Imbaro (Chieti), Italy 2 Department of Biological and Environmental Science, Nanoscience Centre, University of Jyvaskyla, Jyvaskyla, Finland 3 Laboratory of Membrane Traffic, Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Santa Maria Imbaro (Chieti), Italy 4 Theoretical and Computational Membrane Biology, Centre for Bioinformatics, Saarland University, Saarbruecken, Germany To whom correspondence should be addressed Antonino Colanzi, Laboratory of Cell Regulation, Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy. Tel.: +39 0872 570310; Fax: +39 0872 570412; E-mail: colanzi@negrisud.it Alberto Luini, Laboratory of Membrane Traffic, Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy. Tel.: +39 0872 570355; Fax: +39 0872 570412; E-mail: luini@negrisud.it Received 7 September 2007; Accepted 29 February 2008; Published online 20 March 2008. |
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| Abstract |
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| Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surrounding membrane, (b) required for the fission of the macropinocytic cup and (c) phosphorylated on a specific serine that is a substrate for p21-activated kinase, with this phosphorylation being essential for the fission of the macropinocytic cup. Importantly, we also show that CtBP1/BARS is required for macropinocytic internalization and infection of echovirus 1. These results provide an insight into the molecular mechanisms of CtBP1/BARS activation in membrane fissioning, and extend the relevance of CtBP1/BARS-induced fission to human viral infection. |
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| Keywords: CtBP1/BARS, macropinocytosis, membrane fission, Pak1 |
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Top of page MORE ARTICLES LIKE THISThese links to content published by NPG are automatically generated RESEARCHThe closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS The EMBO Journal Article Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3 The EMBO Journal Article Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3 The EMBO Journal Article (09 Apr 2008) |
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