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Biological Chemistry Volume 398 Issue 5-6

Subject Areas: Biochemistry; ;
Publisher: De Gruyter - de Gruyter
ISSN: 1437-4315
SJR: 123

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Frontmatter

2017 Biological Chemistry

doi:10.1515/hsz-2017-frontmatter5-6
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Highlight: GTP- and ATP-dependent membrane processes

2017 Biological Chemistry

doi:10.1515/hsz-2017-0132 pmid:28328522
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Common mechanisms of catalysis in small and heterotrimeric GTPases and their respective GAPs

Gerwert, Klaus; Mann, Daniel; Kötting, Carsten

2017 Biological Chemistry

doi:10.1515/hsz-2016-0314 pmid:28245182

AbstractGTPases are central switches in cells. Their dysfunctions are involved in severe diseases. The small GTPase Ras regulates cell growth, differentiation and apoptosis by transmitting external signals to the nucleus. In one group of oncogenic mutations, the ‘switch-off’ reaction is...
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Structure-based development of PDEδ inhibitors

Martín-Gago, Pablo; Fansa, Eyad Kalawy; Wittinghofer, Alfred; Waldmann, Herbert

2017 Biological Chemistry

doi:10.1515/hsz-2016-0272 pmid:27935847

AbstractThe prenyl binding protein PDEδ enhances the diffusion of farnesylated Ras proteins in the cytosol, ultimately affecting their correct localization and signaling. This has turned PDEδ into a promising target to prevent oncogenic KRas signaling. In this review we summarize and describe the...
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Influence of isoform-specific Ras lipidation motifs on protein partitioning and dynamics in model membrane systems of various complexity

Erwin, Nelli; Patra, Satyajit; Dwivedi, Mridula; Weise, Katrin; Winter, Roland

2017 Biological Chemistry

doi:10.1515/hsz-2016-0289 pmid:27977396

AbstractThe partitioning of the lipidated signaling proteins N-Ras and K-Ras4B into various membrane systems, ranging from single-component fluid bilayers, binary fluid mixtures, heterogeneous raft model membranes up to complex native-like lipid mixtures (GPMVs) in the absence and presence of...
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Mechanisms of action of Rab proteins, key regulators of intracellular vesicular transport

Goody, Roger Sidney; Müller, Matthias Philipp; Wu, Yao-Wen

2017 Biological Chemistry

doi:10.1515/hsz-2016-0274 pmid:27845878

AbstractOur understanding of the manner in which Rab proteins regulate intracellular vesicular transport has progressed remarkably in the last one or two decades by application of a wide spectrum of biochemical, biophysical and cell biological methods, augmented by the methods of chemical...
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The small GTPases Ras and Rheb studied by multidimensional NMR spectroscopy: structure and function

Schöpel, Miriam; Potheraveedu, Veena Nambiar; Al-Harthy, Thuraya; Abdel-Jalil, Raid; Heumann, Rolf; Stoll, Raphael

2017 Biological Chemistry

doi:10.1515/hsz-2016-0276 pmid:28475102

AbstractRas GTPases are key players in cellular signalling because they act as binary switches. These states manifest through toggling between an active (GTP-loaded) and an inactive (GDP-loaded) form. The hydrolysis and replenishing of GTP is controlled by two additional protein classes: GAP...
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Rheb in neuronal degeneration, regeneration, and connectivity

Potheraveedu, Veena Nambiar; Schöpel, Miriam; Stoll, Raphael; Heumann, Rolf

2017 Biological Chemistry

doi:10.1515/hsz-2016-0312 pmid:28212107

AbstractThe small GTPase Rheb was originally detected as an immediate early response protein whose expression was induced by NMDA-dependent synaptic activity in the brain. Rheb’s activity is highly regulated by its GTPase activating protein (GAP), the tuberous sclerosis complex protein, which...
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ATP-driven processes of peroxisomal matrix protein import

Schwerter, Daniel P.; Grimm, Immanuel; Platta, Harald W.; Erdmann, Ralf

2017 Biological Chemistry

doi:10.1515/hsz-2016-0293 pmid:27977397

AbstractIn peroxisomal matrix protein import two processes directly depend on the binding and hydrolysis of ATP, both taking place at the late steps of the peroxisomal import cycle. First, ATP hydrolysis is required to initiate a ubiquitin-transfer cascade to modify the import (co-)receptors....
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When, how and why? Regulated proteolysis by the essential FtsH protease in Escherichia coli

Bittner, Lisa-Marie; Arends, Jan; Narberhaus, Franz

2017 Biological Chemistry

doi:10.1515/hsz-2016-0302 pmid:28085670

AbstractCellular proteomes are dynamic and adjusted to permanently changing conditions by ATP-fueled proteolytic machineries. Among the five AAA+ proteases in Escherichia coli FtsH is the only essential and membrane-anchored metalloprotease. FtsH is a homohexamer that uses its ATPase domain to...

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