- MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 functionVered Maytal-Kivity
Dept of Biology, Institute for Catalysis Science and Technology Technion Israel Institute of Technology, Israel
BMC Biochem 3:28. 2002..In particular Rpn11, a lid subunit, serves as the paradigm for MPN-containing proteins as it is highly conserved and important for proteasome function...
- Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domainTeresa Rinaldi
Pasteur Institute Cenci Bolognetti Foundation and the Department of Cell and Developmental Biology, University of Rome I, 00185 Rome, Italy
Biochem J 381:275-85. 2004..Together, these results point to a unique role for the C-terminal region of Rpn11 in mitochondrial maintenance that may be independent of its role in proteasome-associated deubiquitination...
- COP9 signalosome components play a role in the mating pheromone response of S. cerevisiaeVered Maytal-Kivity
Department of Biology and Institute for Catalysis Science and Technology, Technion Israel Institute of Technology, 32000 Haifa, Israel
EMBO Rep 3:1215-21. 2002..Csi1, a novel CSN interactor, exhibits opposite phenotypes. Deletants also accumulate Cdc53/cullin in a Rub1-modified form; however, this role of the CSN appears to be distinct from that in the mating pathway...
- The COP9 signalosome-like complex in S. cerevisiae and links to other PCI complexesVered Maytal-Kivity
Department of Biology and Institute for Catalysis Science and Technology ICST, Technion Israel Institute of Technology, 32000, Haifa, Israel
Int J Biochem Cell Biol 35:706-15. 2003..Pci8/Csn11 has previously been shown to interact with eIF3. Together, these results point to a network of interactions between these three structurally similar, yet functionally diverse, complexes...