Yeasterday meeting at Leuven

Elie Saliba and Bruno André attended the one-day Yeasterday meeting (May 13), which was organized in Leuven by our colleagues J. Winderickx, K. Verstrepen, and P. Van Dijck. The Yeasterday meeting gathers the research groups of the Benelux working on yeast as a model system.

LMO meeting (Brussels)

DSC_0029Almost all lab members attended the “12th Levures, modèles et outils (LMO)” meeting organized in Brussels. Sir Paul Nurse (Nobel prize 2001) was among the speakers. Melody Cools and Céline Barthelemy, among several other young researchers, were invited to give oral presentations.


Spring Biopark News


Visit the Biopark web site in English or French

“Cystinosis Research Foundation” symposium

Melody Cools and Bruno André attended to the last scientific symposium organized by the “Cystinosis Research Foundation” (Irvine, USA, March 3-4). The meeting gathered all the research groups supported by the CRF and conducting fundamental or clinical research studies on cystinosis, a rare genetic disease caused by mutations in the CTNS gene. This gene encodes a transporter present at the lysosomal membrane and catalyzing export to the cytosol of cystine, the compound made of two cysteines linked by a disulfide bridge. The keynote speaker at the symposium was Dr. Hal Hoffman, a world renowned expert in the field of inflammation.

“Yeast Membrane Transport” book published

A novel review entitled “Function and Regulation of Fungal Amino Acid Transporters: Insights from Predicted Structure” by Gournas C, Kramer M-E, Prévost M & B André has just been published in a Springer book “Yeast Membrane Transport” edited by Ramos, Sychrova and Kschischo, and also appears in “Advances in Experimental Medicine and Biology”.

Winter Biopark News

Visit the Biopark web site in English or French

Florent Corillon obtained a FRIA fellowship

Florent Corillon was informed by the FNRS that he obtained a fellowship from the FRIA. This is an excellent news to close 2015 ! Last year, Florent was hired by the University to work as a research assistant. He could also develop a research project on the role of yeast Gap1 permease in signaling. He’s now going to work full time on his project. Congratulations to him.

New study on traffic of lysosomal transporters in yeast and human cells published in Scientific Reports

A novel paper entitled “The AP-3 adaptor complex mediates sorting of yeast and mammalian PQ-loop-family basic amino acid transporters to the vacuolar/lysosomal membrane” has just been published in the journal Scientific Reports of the Nature publishing group. This article reports converging data obtained in yeast and human cancer cells showing that a similar mechanism based on the AP-3 adaptor complex promotes sorting of basic amino acid transporters (the similar yeast Ypq and human PQLC2 proteins) from the Golgi to the lysosome/vacuole. This work has been carried out by E. Llinares (FRIA PhD student) and A. Barry (FNRS postdoc) in the general context of the study of cystinosis, a genetic disease caused by mutations in the gene encoding cystinosin, the lysosomal exporter of cystine. It was supported by the Cystinosis Research Foundation.

“2015 Cell Biology of Yeast” meeting at Cold Spring Harbor

Elie Saliba, Christos Gournas and Bruno André attended the “Cell Biology of Yeasts” meeting organized at the Cold Spring Harbour Lab congress center (Nov 3-7, 2015). Christos was invited to present a talk at the “Membrane traffic” session about his work on the role of arrestin-like adaptors in ubiquitylation of membrane transporters. We could enjoy top science and the beautiful Fall colors of the campus (see pictures below). This year the Cold Spring Harbor lab celebrated its 125th anniversary.

Stelios Gionis joined the lab

We are pleased to welcome a new pregraduate student, Stelios GIONIS, from the University of Athens (Greece). During his master thesis work, Stelios will investigate the mechanisms of ubiquitylation and endocytosis of the Can1 permease and the links between these mechanisms and the lateral segregation of the protein in the plasma membrane.