Regulation of Normal and Pathologic Processes by Ubiquitin and Ubiquitin-like Proteins: Degradation, Autophagy and Apoptosis (III-S15)

Chairs: Aaron Ciechanover
  Helle Ulrich

July 7, 2013

17.00 - 17.40

Adi Kimchi   Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel

The protein interaction maps of  autophagy and apoptosis and specific points of interface between them

17.40 - 18.05

Kazuhiro Iwai   Department of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University, Kyoto, Japan

Linear polyubiquitination: a new regulator of NF-kappaB activation

18.05 - 18.30

Ivan Dikic   Institute of Biochemistry II, Goethe University School of Medicine, University Hospital, Frankfurt, Germany

Ubiquitin networks in regulation of inflammation and autophagy

18.30 - 18.55

Daniel Finley   Department of Cell Biology, Harvard Medical School, Boston, MA, USA

Recognition and editing of ubiquitin conjugates by the proteasome

18.55 – 19.10

Andriy Sibirny   Department of Molecular Genetics and Biotechnology, Institute of Cell Biology, NAS of Ukraine, Lviv, Ukraine

New genes involved in peroxisome and soluble protein fructose-1,6-bisphosphatase autophagic degradation in yeasts

19.10 – 19.25

Alexey Belogurov   Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia

Ubiquitination is not required for proteasome-mediated degradation of myelin basic protein

19.25 – 19.40

Naveen Kumar Chandappa Gowda    Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University,  Sweden

Two isoforms of Hsp70 nucleotide exchange factor Fes1 are essential for compartment-specific proteasomal degradation of misfolded proteins