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Evelyn Fuchs

Publications and source records attributed to Evelyn Fuchs.

4 recordsLinked to original sources
PubMed2006

Phosphabarrelenes as ligands in rhodium-catalyzed hydroformylation of internal alkenes essentially free of alkene isomerization.

Despite significant research efforts in the past, one of the remaining problems to be solved in industrially important hydroformylation is the chemoselective low-pressure hydroformylation of internal alkenes. We report here on a new class of phosphabarrelene/rhodium catalysts 2 that display very high activity towards hydroformylation of internal alkenes with an unusually low tendency towards alkene isomerization. Preparation of new phosphabarrelene ligands, studies of their coordination properties, as well as results obtained in the rhodium-catalyzed hydroformylation of cyclic and acyclic internal alkenes are reported.

Alkenes↗
PubMed2005

A GTPase-activating protein controls Rab5 function in endocytic trafficking.

Rab-family GTPases are conserved regulators of membrane trafficking that cycle between inactive GDP-bound and activated GTP-bound states. A key determinant of Rab function is the lifetime of the GTP-bound state. As Rabs have a low intrinsic rate of GTP hydrolysis, this process is under the control of GTP-hydrolysis-activating proteins (GAPs). Due to the large number of Rabs and GAPs that are encoded by the human genome, it has proven difficult to assign specific functional relationships to these proteins. Here, we identify a Rab5-specific GAP (RabGAP-5), and show that RN-Tre (previously described as a Rab5 GAP) acts on Rab41. RabGAP-5 overexpression triggers a loss of the Rab5 effector EEA1 from endosomes and blocks endocytic trafficking. By contrast, depletion of RabGAP-5 results in increased endosome size, more endosome-associated EEA1, and disrupts the trafficking of EGF and LAMP1. RabGAP-5 therefore limits the amount of activated Rab5, and thereby regulates trafficking through endosomes.

Adaptor Proteins, Signal Transducing↗
PubMed2005

Assay and properties of rab6 interaction with dynein-dynactin complexes.

RAB GTPases help to maintain the fidelity of membrane trafficking events by recruiting cytosolic tethering and motility factors to vesicle and organelle membranes. In the case of Rab6, it recruits the dynein-dynaction complex to Golgi-associated vesicles via an adaptor protein of the Bicaudal-D family. Here we describe methods for the identification of Rab6-binding partners in cell extracts. We then focus on the biochemical analysis of interactions with the dynein-dynactin complex and the adaptor proteins Bicaudal-D1 and -D2. Standard protocols for yeast two-hybrid analysis, and biochemical assays for the analysis of the interactions between Rab6, Bicaudal-D, and the subunits of the dynein-dynactin complex are outlined.

Dynactin Complex↗