FEBS Letters
FEBS Letters RSS feed. FEBS Letters is one of the world's leading journals in biochemistry and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, hypotheses and research letters that merit urgent publication.FEBS Letters offers:• Faster publication: − Accepted articles are published online in 3 days − The print version of the article is published in 3 to 5 weeks after acceptance• Full-text article disclosure in HTML and PDF formats• Articles in Press are included in PubMed• Easy online manuscript submission system• Transparent online peer review and manuscript tracking system• No page charges• Free color figures Subject Coverage:The subject area of FEBS Letters is broad. It covers biochemistry (including protein chemistry, enzymology, nucleic acid chemistry, metabolism, and immunochemistry), structural biology, biophysics, computational biology (genomics, proteomics, bioinformatics), molecular genetics, molecular biology and molecular cell biology (signal transduction, intracellular traffic, regulation of cellular proliferation, cell-cell interactions) and systems biology. Studies on microbes, plants and animals at the molecular level are within the scope of FEBS Letters.Submitting Authors: Manuscripts can be submitted to FEBS Letters at: http://ees.elsevier.com/febsletters/
Updated: 8 years 21 weeks ago
The K-uptake permease 7 (AtKUP7) contains a functional cytosolic adenylate cyclase catalytic centre
Adenylate cyclases (ACs) (EC 4.6.1.1) catalyze the formation of the universal second messenger cyclic adenosine 3′, 5′-monophosphate (cAMP) from adenosine 5’-triphosphate. Cyclic AMP participates in key signal transduction pathways in all living organisms ranging from the simple prokaryotes such as Escherichia coli to complex multicellular organisms including Homo sapiens. Cyclic AMP was first discovered in eukaryotic cells as the factor that mediates the effects of hormones [1] while in lower eukaryotes including slime molds and fungi, cAMP regulates signaling pathways [2] that are critical for adaptation and survival [3–5].
Uncoupling phototoxicity-elicited neural dysmorphology and death by insidious function and selective impairment of Ran-binding protein 2 (Ranbp2)
Morphological disintegration of neurons invariably triggers neural death and is a hallmark feature of neurodegeneration [1–6]. Photoreceptors neurons are the primary photon-capturing neurons of the retina. In particular, the outer segment (OS) structures of photoreceptors undergo degeneration owing to intrinsic (e.g. genetic mutations) or extrinsic (e.g. environmental) pathological stimuli [5,6]. Light-stress is a powerful and extrinsic deleterious stressor that promotes the dysplasia of the OS of photoreceptors and ultimately photoreceptor death [7–13].
Commitment of Annexin A2 in recruitment of microRNAs into extracellular vesicles
Small non-coding RNA microRNAs (miRNAs) regulate gene expression at the post-transcriptional level by binding sequence-specific sites within the 3′ untranslated region of target mRNAs [1]. In addition, miRNAs can fine-tune various biological processes, including development, organogenesis, metabolism, and homeostasis [2]. miRNAs have been found in human body fluids despite the abundant presence of ribonucleases (RNases) [3]. This finding has led to the proposal of a scenario in which miRNAs could be packaged in certain RNase-resistant containers when they are secreted out of cells.
Role of cytosolic and calcium independent phospholipases A in insulin secretion impairment of INS-1E cells infected by
Phospholipases A2 (PLA2) are a large family of enzymes ubiquitously expressed that catalyze the breakdown of glycerophospholipids, releasing arachidonic acid (AA): cytosolic PLA2 (cPLA2), Ca2+-independent PLA2 (iPLA2), and Ca2+-dependent secretory PLA2 (sPLA2) differ from each other in terms of substrate specificity and Ca2+-requirement [1]. The cPLA2, present in many cell types, including pancreatic β cells (cPLA2β), requires phosphorylation at Ser505 and binding with Ca2+ for its activity. Activation of cPLA2β would cause translocation of the enzyme to the secretory granules and accumulation of AA and lysophospholipids in the membrane, leading to changes in membrane structure or fluidity [2].
Characterization and crystal structure determination of β-1,2-mannobiose phosphorylase from
Glycoside phosphorylases (GPs) are useful tools for efficient oligosaccharide synthesis because of the reversible nature of their reactions [1–3]. Although increasing numbers of GPs have been reported recently, their utilization for the production of various oligosaccharides remains limited by the extent of known and characterized enzymes. In the Carbohydrate-Active enZyme database [4], anomer-inverting GPs are all categorized into glycoside hydrolase (GH) families: GH65, GH94, GH112, and GH130.
EZH2 phosphorylation regulates Tat-induced HIV-1 transactivation via ROS/Akt signalling pathway
EZH2 plays a major role in HIV-1 latency, the molecular linkage between Tat-induced HIV-1 transactivation and EZH2 activity, is not fully understood. It was shown Tat-induced HIV-1 transactivation through inhibiting EZH2 activity. Tat decreased the levels of H3K27me3 and EZH2 occupy at the long terminal repeat (LTR) of HIV-1. We further showed for the first time that transfected with Tat construct resulted in an increase in phosphorylated EZH2 (p-EZH2), mediated by active Akt. ROS/Akt-dependent p-EZH2 was correlated with Tat-induced transactivation.
Mapping the heparin-binding site of the osteoinductive protein NELL1 by site-directed mutagenesis
Neural epidermal growth factor-like (NEL)-like 1 (NELL1), encodes a large secretory glycoprotein that was first identified as a gene overexpressed in human sporadic coronal craniosynostosis. NELL1 is expressed primarily in developing and adult brain [1,2]. Transgenic mice overexpressing NELL1 exhibit premature cranial suture closure with bone overgrowth similar to human craniosynostosis patients, whereas NELL1-deficient mice result in cranial and vertebral skeletal defects, suggesting that NELL1 functions as a regulator of craniofacial skeletal morphogenesis [3–5].
Crystal structure of the Z-ring associated cell division protein ZapC from
Most bacteria and archaea divide using a contractile septal ring that is composed of intracellular or inner, cytosolic proteins, including the bacterial tubulin homologue FtsZ, and also middle, transmembrane proteins and outer, periplasmic proteins [1–3]. Together, the putative protein complexes involved in this process have been termed the divisome [4]. The inner divisome proteins organise into a ring structure, the Z-ring that is used as a platform to recruit the downstream components of the system including the transmembrane and periplasmic proteins [5].
Variable reproducibility in genome-scale public data: A case study using ENCODE ChIP sequencing resource
The ENCODE project has set up a model to generate large data to understand mammalian transcription control by pooling resources across the globe. The easy accessibility of these data, including processed files, has resulted into many researchers world-wide using the ENCODE resource to learn new biology, either by integrating existing data [1] or by integrating with their own new data [2]. An especially valuable part of the ENCODE resource concerns the identification of the binding sites of transcription factors and chromatin modifiers at genome-wide scale using chromatin immuno-precipitation (ChIP) followed by high throughput sequencing (ChIP-seq).
Specific mutations in mammalian P4-ATPase ATP8A2 catalytic subunit entail differential glycosylation of the accessory CDC50A subunit
P4-ATPases, or flippases, translocate phospholipids from cytoplasmic to exoplasmic membrane leaflets of eukaryotic biological membranes [1–3]. Flippases are essential for creating and maintaining the asymmetry between the two leaflets. Several of the 14 mammalian flippases have been causally linked to severe disorders [4–10], and human flippases as well as flippases of parasites are involved in resistance toward chemotherapy and anti-infectious drugs, respectively [11–15]. Hence, understanding the flippase structure and mechanism is of great interest.
Cystatin C attenuates insulin signaling transduction by promoting endoplasmic reticulum stress in hepatocytes
Cystatin C (Cys C) is a potent extracellular inhibitor of cysteine protease, and has been generally considered a ubiquitously expressed protein as no obvious regulatory elements were found in its gene promoter [1]. Cys C is described as the more accurate marker of renal function impairment, especially at very early stages of chronic kidney disease [2,3], as this 13.3kDa protein is almost completely cleared from the circulation by glomerular filtration [4]. Recently, a growing number of evidences have shown that the plasma levels of Cys C predict incident of type 2 diabetes.
Pc2-mediated SUMOylation of WWOX is essential for its suppression of DU145 prostate tumorigenesis
WWOX, a tumor suppressor gene spanning chromosomal fragile site FRA16D, which encodes 414 amino acids contains two typical N-terminal WW domains, one C-terminal short-chain dehydrogenase reductase (SDR) domain, and one nuclear localization sequence (NLS) [1]. Previous studies have suggested that WW domains of WWOX, which consist of 35 amino acids having two signature tryptophan (W) residues bind to PPXY-containing proteins [2,3]. WWOX protein is known to be implicated in several cellular events including cancer cell apoptosis and tumor suppression [1].
Characterization of ClpS2, an essential adaptor protein for the cyanobacterium
AAA+ proteases such as the 26S proteasome and Clp proteases fulfill an important role in maintaining cell viability. Clp are a family of serine-type proteases found in a wide range of organisms, ranging from all eubacteria to vascular plants and mammals. Their general architecture is a hexameric ATPase ring that unfolds the bound protein substrate and then delivers it to the proteolytic partner, which consists of two opposing heptameric rings of ClpP subunits. Two distinct Clp proteases exist in Escherichia coli based on their different chaperone ATPase components, ClpXP and ClpAP [11,36].
Calcium ions inhibit reduction of heme in bovine cytochrome c oxidase
Cytochrome c oxidase (CcO) is a terminal component of the respiratory chain of mitochondria and many bacteria. The enzyme gates access of oxidative phosphorylation to oxygen as the final electron acceptor. CcO catalyzes electron transfer (ET) from ferrous cytochrome c to oxygen, and free energy of this thermodynamically favourable process is conserved in a form of transmembrane difference of proton electrochemical potential, ΔμH+ (reviewed, [1–3]).
Mass spectrometry cancer data classification using wavelets and genetic algorithm
Mass spectrometry (MS) is a powerful analytical chemistry technique that was initially introduced to determine the constituent elements of small molecules. Mass spectrometers consist of three main parts: an ion source, a mass analyser, and an ion detection system [1]. Components of a sample mixture are converted to ions, which are then bombarded with an electron beam having sufficient energy. In Fig. 1, the high voltage beams are to accelerate the ions in the target sample so that they all have the same kinetic energy.
Insights into the behavioral difference of water in the presence of GM1
Water is the most crucial constituent of lipid membranes, whose interaction is essential to maintain the structure and function of cell membrane [1–4]. Depending on the location in the lipid membrane, water molecules reveal very diverse properties [5] and a number of classifications is considered such as bulk, interfacial, bound and penetrating water according to their position in lipid membrane [6–8].
A bacterial homologue of the human iron exporter ferroportin
Ferroportin (Fpn) is a key player in maintenance of iron homeostasis because it is the sole iron exporter so far identified in vertebrates. Missense mutations of Fpn lead to “ferroportin disease”, or type 4 hemochromatosis, characterized by dominant inheritance and by two distinct phenotypes in terms of iron accumulation depending on whether the mutation affects the activity or the degradation pathway of Fpn ([1] and Refs. therein). Binding of the peptide hepcidin induces internalization and degradation of Fpn [2], thus limiting iron export from cells.
miR-190a inhibits epithelial–mesenchymal transition of hepatoma cells via targeting the long non-coding RNA treRNA
Hepatocellular carcinoma (HCC) is the most common type of cancers worldwide, with the highest morbidity in Asia and Sub-Saharan Africa [1]. Remarkably, China alone accounts for ∼50% of all HCC cases [2]. Viral hepatitis infection (the hepatitis B or C viruses, HBV or HCV), alcohol abuse and exposure to dietary aflatoxin B have been identified as important etiological risk factors of HCC. However, only a portion of exposed individuals finally developed HCC, indicating that genetic makeup may also contribute to HCC etiology [3].
Structural in silico dissection of the collagen V interactome to identify genotype–phenotype correlations in classic Ehlers–Danlos Syndrome (EDS)
Ehlers–Danlos Syndrome (EDS) (OMIM 130000) is a group of heritable connective tissue disorders, characterized by skin hyperelasticity, joint hypermobility and general tissue fragility [1] and the pathogenic mechanisms leading to EDS remain unclear. The syndrome is a complex and heterogeneous disorder showing subtypes with heterogenic clinical manifestations. The various EDS subtypes are generally associated to collagen defects, yet mutations in different extracellular matrix (ECM) proteins, e.g.