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 20 weeks ago
Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross-β region
Proteins adopt stable structures conducive to biological functions. Amyloids, unlike natively folded proteins, form through protein misfolding and are associated with physiological dysfunction. Amyloids are formed by the aggregation of amyloid fibrils. Although there is variation in the native three-dimensional structures of amyloid fibrils, they are typically 10nm in diameter, long, and unbranched [1]. Amyloid fibril formation is associated with a variety of diseases, including Alzheimer’s disease, prion diseases, and dialysis amyloidosis, which are generally termed conformational diseases because of being caused by changes in the structure or conformation of proteins [2–4].
Transcriptional analysis of the gene uncovers novel isoforms expressed during development in
Numerous tissues undergo an additional level of organization through an evolutionary conserved mechanism called planar cell polarity (PCP), which contributes to the development of fully functional organs of a precise size and shape. The Drosophila cadherin-related Dachsous (Ds) and Fat (Ft) proteins and their homologues in vertebrates participate in the control of PCP and growth (reviewed in [1]). The current model is based on the heterophilic interaction between these two single-pass transmembrane proteins.
Immediate-early response 5 (IER5) interacts with protein phosphatase 2A and regulates the phosphorylation of ribosomal protein S6 kinase and heat shock factor 1
Protein phosphatase 2A (PP2A) is a ubiquitously expressed, highly abundant serine/threonine phosphatase and accounts for the majority of serine/threonine phosphatase activity in most cells [1–3]. The catalytic C subunit is associated with the scaffold A subunit, consisting of the core of the enzyme. The core enzyme binds to the regulatory B subunit, which consists of a family of more than 20 proteins, forming a trimeric holoenzyme. There are four B subunit subfamilies: B/B55/PR55, B′/B56/PR61, B″/PR72, and B′″/PR93/PR110.
Cysteine is not a substrate but a specific modulator of human ASCT2 (SLC1A5) transporter
The Alanine Serine Cysteine Transporter 2 (ASCT2; SLC1A5) belongs to the SLC1 family that includes another neutral amino acid transporter (ASCT1) sharing less than 60% identity with ASCT2, and five glutamate transporters [1,2]. Over the years, it was demonstrated that ASCT2 catalyzes a strictly sodium-dependent antiport in which Na+ together with an extracellular neutral amino acid are exchanged with an internal amino acid. The peculiar three substrate mechanism has been firstly investigated in intact cells [3] and then extensively characterized in proteoliposome models reconstituted with the rat protein [4] or with the recombinant human protein over-produced in yeast [5,6].
Systemic control of protein synthesis through sequestration of translation and ribosome biogenesis factors during severe heat stress
Eukaryotic cells respond to changes in their environment not only by altering their gene expression program, but also by reorganizing the subcellullar distribution of their components. For instance, the assembly of stress granules (SGs) in the cytoplasm represents a conserved mechanism to control protein synthesis under a variety of stress conditions [1]. The deposition of translationally repressed mRNAs and translation factors in SGs regulates protein synthesis during stress periods and facilitates cell recovery upon stress relief [2].
Alzheimer’s disease is associated with disordered localization of ganglioside GM1 molecular species in the human dentate gyrus
Alzheimer’s disease (AD) is a progressive dementia associated with loss of memory and cognitive dysfunction [1]. One of pathophysiological hallmarks of AD is extracellular amyloid β-peptide (Aβ) aggregation in the form of amyloid plaques [2,3]. The presence of Aβ-producing secretases in lipid rafts [4,5] supports the involvement of lipid rafts in the processing of amyloid precursor protein (APP) [6]. Gangliosides are glycosphingolipids that contain sialic acid in oligosaccharide chains and constitute lipid rafts [7,8].
Agonist mobility on supported lipid bilayers affects Fas mediated death response
Programmed cell death (extrinsic apoptosis) is an active process in which cells disintegrate in an orchestrated and regulated fashion initiated by distinct signalling cascades. In particular Fas receptor (CD95, Apo1) mediated apoptosis is important for tissue maintenance and renewal, embryonic development, the control of cell proliferation in epithelia and the immune system, as well as for pathological situations such as viral infections, autoimmune and neurodegenerative diseases [1–3]. Upon Fas activation, apoptotic cells undergo global morphological changes such as chromatin condensation, loss in cytoskeletal organization, and membrane blebbing [4,5].
An inverting β-1,2-mannosidase belonging to glycoside hydrolase family 130 from
Glycoside phosphorylases are useful catalysts for practical preparation of oligosaccharides [1–3]. These enzymes are categorized into the following families in CAZy database (http://www.cazy.org/) [4]: glycosyltransferase (GT) 4 and 35, and glycoside hydrolase (GH) 3, 13, 65, 94, 112, and 130. Several new activities of phosphorylases have been identified in the past decade through the exploration in such families [5,6].
MiR-455-3p regulates early chondrogenic differentiation via inhibiting Runx2
MicroRNAs (miRNAs) are a group of non-coding, single stranded, small RNAs (∼22 nt in length) that have been identified as important post-transcriptional regulators [2]. MiRNAs function as regulators in gene silencing by binding to the 3′-untranslated region (3′UTR) of target mRNAs, leading to translational repression. miRNAs have been reported to have important roles in multiple biological processes, including the process of cartilage differentiation and degradation [1,3–7,38–40]. Dicer is an essential component for the biogenesis of miRNAs, and Dicer-null growth plates showed a progressive reduction in the proliferation of chondrocytes and the acceleration of hypertrophy, leading to severe skeletal growth defects and premature death in mice [8].
Editorial
In the last fifteen years South America has experienced a favourable scientific development contributing valuable research in various fields of the life sciences. In this stimulating context, South American based scientists have substantially increased their rate of publication in the recent years. The present South America Special Issue aims at bringing together for the first time into a single volume a sample of current research in life sciences carried out in the region. We have assembled what we believe is a reputable group of innovative and interdisciplinary researchers, who contributed reviews in a broad range of disciplines in the life sciences, particularly Neuroscience, Molecular, Structural and Stem Cell Biology, Immunology and Cancer.
The evolution of Class II Aminoacyl-tRNA synthetases and the first code
The extant Aminoacyl-tRNA synthetases, (aaRS), carry out the initial critical steps in the translation of the Genetic Code. This code is the mapping from the four nucleotides (GCAU) alphabet to the 20 amino acids. The synthetases carry out this mapping by activating and then attaching each particular amino acid to its cognate tRNA [1]. This is a two reaction process; first the amino acid is activated with ATP to form an Aminoacyl-AMP and then the activated amino acid is transferred to the 3′ OH of the terminal Adenosine of their cognate tRNA.
The role of retinal light induced dipole in halorhodopsin structural alteration
Halorhodopsin (HR), a member of archaeal rhodopsins contains retinal chromophore bound via a protonated Schiff base to the ε-amino group of a lysine residue. The photoisomerization reaction around the C13C14 double bond triggers a series of conformational changes by which a chloride ion is transported [1–3]. The HR homologs from Halobacterium salinarum (shR) and Natronomonas pharaonis (phR) were extensively studied [4–10]. These HR homologs investigated so far differs in many aspects. They have low sequence identity (55%) which is subsequently reflected in profound differences in their ion specificity, spectroscopic property and kinetic behavior.
Laminin therapy for the promotion of muscle regeneration
Muscle regeneration is essentially due to activation of satellite cells, which can be isolated and amplified ex vivo, thus representing good candidates for cell therapy. Accumulating data show that the local microenvironment plays a major role during muscle regeneration. In the satellite cell niche, a major extracellular matrix protein is laminin. Human myoblasts transplanted into immunodeficient mice are preferentially located in laminin-enriched areas. Additionally, laminin-111 enhances myoblast proliferation in vitro and increases expression of the α7β1 integrin-type laminin receptor.
Computational prediction of protein interfaces: A review of data driven methods
Reliably pinpointing which specific amino acid residues form the interface(s) between a protein and its binding partner(s) is critical for understanding the structural and physicochemical determinants of protein recognition and binding affinity, and has wide applications in modeling and validating protein interactions predicted by high-throughput methods, in engineering proteins, and in prioritizing drug targets. Here, we review the basic concepts, principles and recent advances in computational approaches to the analysis and prediction of protein–protein interfaces.
Dissecting the role of Engrailed in adult dopaminergic neurons – Insights into Parkinson disease pathogenesis
The homeoprotein Engrailed (Engrailed-1/Engrailed-2, collectively En1/2) is not only a survival factor for mesencephalic dopaminergic (mDA) neurons during development, but continues to exert neuroprotective and physiological functions in adult mDA neurons. Loss of one En1 allele in the mouse leads to progressive demise of mDA neurons in the ventral midbrain starting from 6weeks of age. These mice also develop Parkinson disease-like motor and non-motor symptoms. The characterization of En1 heterozygous mice have revealed striking parallels to central mechanisms of Parkinson disease pathogenesis, mainly related to mitochondrial dysfunction and retrograde degeneration.
Diversity and development of local inhibitory and excitatory neurons associated with dopaminergic nuclei
For regulation of voluntary movement and motivation the midbrain dopaminergic system receives input from a variety of brain regions. Often this input is mediated by local non-dopaminergic neurons within or closely associated with the dopaminergic nuclei. In addition to the dopaminergic neurons, some of these non-dopaminergic neurons also send functionally important output from the ventral midbrain to forebrain targets. The aim of this review is to introduce subtypes of GABAergic and glutamatergic neurons, which are located in the dopaminergic nuclei or the adjacent brainstem and are important for the regulation of the dopaminergic pathways.
Crystal structure of the bacteriophage P2 integrase catalytic domain
The addition, deletion and modification of genes in bacteria, fungi, other microorganisms and higher eukaryotes play important roles in genome evolution and in processes such as viral infection, replication and DNA repair, in addition to being useful tools in research, drug development and biotechnology.
Genome-wide analysis of alternative splicing events in : Highlighting retention of intron-based splicing and its possible function through network analysis
The presence of introns within a protein-coding gene can generate more than one mRNA isoform through an event called as alternative splicing (AS). This process increases the transcriptome plasticity and proteome diversity without increasing the gene content [1]. In some cases, alternatively spliced pre-mRNAs may yield thousands of splice variants [2]. To date, four main types of AS are known: exon skipping, alternative 5′ splice site, alternative 3′ splice sites and intron retention [3].
STIM1 is cleaved by calpain
Ca2+ ions serve as versatile intracellular messengers; as such, the cell has evolved various pathways to properly control the movement of Ca2+ ions across various membranes and the accumulation of ions within cellular organelles. One such pathway is store-operated calcium entry (SOCE), which couples depletion of ER luminal Ca2+ stores with Ca2+ influx across the plasma membrane [1]. SOCE is mediated by two key proteins: stromal interaction molecule 1 (STIM1), an ER transmembrane protein serving as a Ca2+ store sensor [2,3]; and calcium release-activated calcium channel (Orai) family membrane proteins, which serve as plasma membrane Ca2+ channels [4].
SMIM1 is a type II transmembrane phosphoprotein and displays the Vel blood group antigen at its carboxyl-terminus
Small integral membrane proteins (SMIMs) constitute a collection of currently 24 unrelated proteins with a single predicted transmembrane domain and a low theoretical molecular mass (6.9–18.4kDa). The genes encoding SMIMs were recently included in the annotation of the human genome by the Human Gene Organization (HUGO) given experimental evidence emerged for the existence of their encoded proteins, primarily by mass spectrometry. Outside of the field of peptide hormone research, very small proteins encoded by the genome have been rather neglected, with most SMIMs remaining as uncharacterized proteins.