Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The second Keystone Symposium on AAA+ proteins, “AAA+ Proteins: From Atomic Structures to Organisms”, was held in Tahoe City, USA in January 2020. The program highlighted recent advances from structural, biochemical and cellular approaches that have extended our understanding of these important ATP-driven molecular machines.
The Ninth International Conference on the Hsp90 Chaperone Machine concluded in October 2018, in Leysin, Switzerland. The program highlighted findings in various areas, including integrated insights into the molecular mechanism of Hsp90, cochaperones, and clients’ structure and function.
Cells rely on the synthesis, translocation, folding and turnover of proteins. Owing to complexity, spatiotemporal regulation and surveillance of these processes are vital. Advances in the field were discussed at the international symposium ‘Proteins: From the Cradle to the Grave’ that took place in the wonderful setting of a Buddhist temple located close to Kyoto, Japan. The emerging theme was the interdependence among cellular processes and organelle compartments.
A symposium in June 2018 sponsored by the Center on Membrane Protein Production and Analysis, a unit of the New York Structural Biology Center, focused on the structures of proteins residing in biological membranes. Explicit emphasis was placed on currently developing technologies aimed at determining such structures and at understanding their dynamics, mechanisms and complex interactions.
The number of conferences on epigenetics has been increasing in the past decade, underscoring the impact of the field on a variety of areas in biology and medicine. However, the mechanistic role of the epigenome in adaptation and inheritance, and how the environment may impinge on epigenetic control, are topics of growing debate. Those themes were the focus of the inaugural international King Abdullah University of Science and Technology (KAUST) Research Conference on Environmental Epigenetics in Saudi Arabia, where more than 100 participants from 19 countries enjoyed vibrant scientific discussions and a pleasant February breeze from the Red Sea.
The Eighth International Conference on the Hsp90 Chaperone Machine took place in November 2016 at the Seeon Abbey in Germany. This year's program focused on a variety of topics, reflecting Hsp90's diverse roles in cellular and physiological function. The highlights included structural insights into the Hsp90 folding mechanism and conformational dynamics, post-translational modifications, client protein maturation, Hsp90 cochaperone function and Hsp90's role in disease physiology.
During protein synthesis, the growing nascent polypeptide chain acts as a positive or negative regulator of the rate of peptide-bond formation and ribosomal fidelity, and influences the efficiency of downstream protein-folding and targeting events. At a recent international meeting held on the banks of Lake Kawaguchi in Japan, scientists and students investigating diverse aspects of nascent-chain biology met to discuss their latest findings in the scenic presence of Mount Fuji.
The Seventh International Conference on the Hsp90 Chaperone Machine took place in October 2014, in Seeon, Germany. The program highlighted recent findings in a variety of areas, including structures of heat-shock protein 90 (Hsp90)–client protein complexes, coordination of Hsp90 with cochaperones, new cellular and physiological roles for Hsp90 and therapeutic targeting of the Hsp90 ensemble for the treatment of disease and prevention of infection.
The Sixth International Conference on Hsp90 in 2012 revealed new functions of this key molecular chaperone. Attendees of the meeting at Les Diablerets, Switzerland, addressed new discoveries about Hsp90 and its cochaperones.
The health of the proteome in the face of multiple and diverse challenges directly influences the health of the cell and the lifespan of the organism. A recent meeting held in Nara, Japan, provided an exciting platform for scientific exchange and provocative discussions on the biology of proteins and protein homeostasis across multiple scales of analysis and model systems.
Heat shock protein 90 (Hsp90) was the focus of a recent meeting in the Swiss Alps, where the Hsp90 community met to discuss the operation and functions of this ubiquitous and essential molecular chaperone.
Hsp90s, molecular chaperones critically involved in many essential cellular processes, were the focus of a recent international conference held in Seeon, Germany. The scope of the conference ranged from structural and mechanistic insights all the way to medical applications.
Structural biology is making significant contributions toward an understanding of molecular constituents and mechanisms underlying human diseases at an atomic resolution, as discussed at the international Murnau Conference on Structural Biology of Disease Mechanisms held in September 2007 in Murnau, Germany.
The Protein Structure Initiative of the US National Institutes of Health has entered its second year. Its status is reported here, as discussed at December's meeting of the principal investigators.
An international conference focusing on the Hsp90 molecular chaperone was recently held in Seeon, Germany. The program provided a current synopsis on a wide array of topics, including structural insights, roles in established and novel cellular pathways and disease implications.
Over the next few years, structural proteomics will grapple with the problem of visualizing increasingly elaborate structures, from the atomic details of protein structures up to subcellular structures and the whole cell. A recent EU workshop addressed the question of what experimental and theoretical approaches, technologies and infrastructures this will demand.
RNA localization and translational control are crucial for cellular fine-tuning of gene expression in space and time. A recent meeting in Tucson, Arizona pointed out mechanisms conserved across different species and cell types that contribute to the establishment of cell polarity and cell migration. Furthermore, it is becoming increasingly clear that these post-transcriptional control processes are relevant for various diseases.
A recent international conference focused on Hsp90, a molecular chaperone that plays a critical role in a diverse array of cellular processes including the assembly and maturation of some important 'client' proteins, many of which are involved in signal transduction.
In a spectacular location nestled in the hills on Croatia's coast, a group of ∼300 scientists from around the world gathered to listen to recent advances in cellular signaling and to gaze across the Adriatic Sea during discussions that surely put this work into perspective. Topics discussed ranged from precise structural details of signaling events to animal models for understanding signaling disorders.
Gene expression is a highly interconnected multistep process. A recent meeting in Iguazu Falls, Argentina, highlighted the need to uncover both the molecular details of each single step as well as the mechanisms of coordination among processes in order to fully understand the expression of genes.