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This year the FEBS Congress is taking place in Jerusalem, an emblematic historical city where different religions and civilizations meet. Throughout the centuries, Jerusalem has hosted numerous leading figures in many areas of arts and sciences. The names and activities of several Nobel laureates are associated with this city and the Hebrew University of Jerusalem. The renowned physicist Albert Einstein was one of the founders of this University, and was highly engaged in its development. Today the Hebrew University of Jerusalem hosts more than 2000 papers and personal belongings of Einstein’s in the Einstein Archives, a recommended destination to everyone visiting Jerusalem. The FEBS Congress will present nearly the entire spectrum of molecular life sciences in more than 20 symposia. The present Special Issue features Review articles reflecting this wide range of topics and provides the reader with a broad overview of what will be discussed at the Congress. The first two articles both relate to cellular 3D structures. Goodstadt and Marti-Renom discuss the complexity of 3D representations of genomes and the challenges related to the visualization of novel spatial data [1]. A completely different way to approach 3D views is cryo-electron tomography. Wagner and colleagues review recent technological developments, such as Volta phase plate or cryo-focused ion beam milling, that have emerged for visualizing high-resolution cellular structures and allow for structural studies in unprecedented detail [2]. Stress granules represent a particular aspect of mRNA localization. The location and timing of their formation, as well as the mechanisms through which mRNA–protein complexes accumulate and interact with stress granules are discussed by Steinberger and Shav-Tal [3]. A number of Review articles focus on various signaling processes, such as Death Receptor 3 signaling and its function in the immune system (Bittner and Ehrenschwender) [4]; the structure–function relationship of ion channel transporters and their role in cell signaling (Abbott) [5]; new approaches to identify regulatory kinases by phospho-proteomics (Dermit et al.) [6]; the mammalian central satiety pathway involving hypothalamic neurons in the arcuate nucleus (Rubinstein and Low) [7]; and a searchable database of ERK target proteins based on phospho-proteomic technology ( € Unal et al.) [8]. A further set of Review articles covers protein degradation and homeostasis. A major well-known degradation pathway is the ubiquitin/proteasome system in which numerous E3 ubiquitin ligases collaborate with molecular chaperones to recognize and degrade their substrates and, in case of malfunctioning, give rise to pathological conditions (Kevei et al.) [9]. A detailed Review on HECT E3 ligases addresses how the catalytic activity of Nedd4 family members is regulated (Fajner et al.) [10]. The role of the molecular chaperone Hsp70 in protein substrate degradation is shown to involve a combination of interacting partners, co-chaperones, and other chaperones (Fern andezFern andez et al.) [11]. Oxidative protein folding occurs in the bacterial periplasm, the ER and the mitochondrial intermembrane space. How the redox balance in these structures is maintained, and how important it is for proper cell functioning, is discussed by Cardenas-Rodriguez and Tokatlidis [12]. In addition, the Review by Jores and Rapaport [13] examines the early steps that determine proper localization of b-barrel proteins at the outer mitochondrial membrane. Finally, Miskei and colleagues [14] report on how intrinsic disorder is a prerequisite for proteins to undergo structural dynamic transitions in order to accommodate to their cellular requirements. FEBS Letters highly appreciates the outstanding organization of the 42nd FEBS Congress by the Israeli Society of Biochemistry and Molecular Biology. The conference provides a vibrant forum bringing together scientists from all over the world to discuss their ideas with Israel’s biochemists. Last but not least FEBS Letters thanks all authors that have contributed to this Special Issue and acknowledges their efforts in sharing their work and ideas with the scientific community.