FEBS Press is pleased to welcome its fourth journal, Molecular Oncology, to this platform. Molecular Oncology is now fully Open Access and all content from the past 10 years is now available for all to read. The publication of high-quality journals by scientists for scientists is one the core objectives of The Federation of European Biochemical Societies (FEBS), with the revenue raised supporting fellowships, courses, congresses and other activities.
The dock-and-coalesce mechanism for the association of a WASP disordered region with the Cdc42 GTPase
Zhou and colleagues, The FEBS Journal
Intrinsically disordered proteins (IDPs) undergo folding upon binding to their interacting partners. Using the Wiskott-Aldrich Syndrome protein (WASP) and its binding partner, the Cdc42 GTPase, Zhou and colleagues show that binding begins with diffusion-dependent docking between the intrinsically disordered GTPase-binding domain (GBD) of WASP and its cognate binding site on Cdc42, and subsequently the remaining segments of WASP coalesce around their Cdc42 subsites. The authors also show that the rate of the docking step is the main contributor to the association rate constant of this two-step binding process.
Burridge, The FEBS Journal
Focal adhesions are sites of interaction between the actin cytoskeleton and the extracellular matrix mediated by clustered integrin receptors on the plasma membrane. In this Discovery-in-Context Review, Keith Burridge provides a personal account on the development of the field of focal adhesion research, beginning with the initial description of focal adhesions almost 50 years ago, to the identification of the structural components of focal adhesions and their role in many signalling pathways.
hSnd2 protein represents an alternative targeting factor to the endoplasmic reticulum in human cells
Lang, S. and colleagues, FEBS Letters
The SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) pathways target proteins to the endoplasmic reticulum (ER). Another ER-targeting pathway, SRP-independent (SND), has been identified in yeast. Here, the authors present the first functional characterization of a human SND pathway component, hSND2. An ER membrane protein, hSnd2 preferentially targets proteins with a C-terminal transmembrane domain. The study provides insights into distinct and overlapping functions of the ER-targeting routes.
Dissecting the structure-function relationship in lysozyme domain of mycobacteriophage D29-encoded peptidoglycan hydrolase
Jain, V. and colleagues, FEBS Letters
Bacteriophage lysins degrade bacterial cell wall peptidoglycans during virion release. Here, Joshi et al. characterize the central lysozyme domain of Mycobacteriophage D29 Lysin A, which can hydrolyze peptidoglycans of both Gram-positive and Gram-negative bacteria. The authors map the active site and identify critical residues conferring stability and functionality. The results might enable the development of mycobacteriophage-based broad-spectrum antibacterials.
A uremic toxin (indoxyl sulfate) found in chronic kidney disease supresses bone formation and resorption
Inada and colleagues, FEBS Open Bio
Patients with chronic kidney disease (CKD) often present with bone turnover abnormalities, which has been associated with low serum levels of parathyroid hormone (PTH). Here, Inada and colleagues report that Indoxyl sulphate (IS), a uremic toxin known to accumulate in the blood of CKD patients, directly supresses osteoblast/osteoclast coupling and bone formation in vitro. This, combined with their previous findings that showed IS exacerbated low bone turnover induced by parathyroidectomy suggests that IS directly induces low bone turnover via the inhibition of bone formation using mechanisms separate from skeletal resistance to parathyroid hormone (PTH). This suggests IS initiates low-turnover bone disease in patients with CKD via a direct action upon both osteoclast precursors and osteoblasts to supress bone formation and resorption.
Hombach-Klonisch and colleagues, Molecular Oncology
Dovitinib (Dov), an FDA- approved oral drug, is able to cross the blood-brain barrier and has recently demonstrated promising efficacy in clinical trials for glioblastoma (GB) patients with recurrent disease. The Dov-mediated molecular mechanisms in GB cells remained unknown. Here, Hombach-Klonisch and colleagues show that Dov treatment attenuated the STAT3/LIN28/Let-7/HMGA2 regulatory axis in GB cells, and downregulated key base excision repair factors known to repair temozolomide (TMZ) induced DNA damage. Dual or sequential treatment with Dov and TMZ enhanced the efficacy of TMZ, reduced GB cell survival, growth, and self-renewal capacity and severely compromised the recovery of GB cells. Alternate administration of Dov and TMZ may improve therapeutic efficacy, especially in patients expected to exhibit increased TMZ resistance. These findings suggest ‘Dov priming’ is an encouraging novel therapeutic strategy to improve the efficacy of TMZ in patients with GB.
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