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1.  Flagging the Fatty Acid Ferryman 
PLoS Biology  2015;13(2):e1002054.
Fatty acids made in chloroplasts must be exported into the rest of the cell to be converted into commercially important plant oils. A new study identifies FAX1 as a protein that mediates this crucial transport step. Read the Research Article.
doi:10.1371/journal.pbio.1002054
PMCID: PMC4315455  PMID: 25646782
2.  What Goes “99-Thump?” 
PLoS Biology  2014;12(11):e1002006.
doi:10.1371/journal.pbio.1002006
PMCID: PMC4244034  PMID: 25422891
3.  Living in Constant Crisis—When Stress Management Becomes the Problem 
PLoS Biology  2014;12(11):e1001999.
doi:10.1371/journal.pbio.1001999
PMCID: PMC4236009  PMID: 25405339
4.  Symbiosis Plasmids Bring Their Own Mutagen to the Wedding Party 
PLoS Biology  2014;12(9):e1001943.
doi:10.1371/journal.pbio.1001943
PMCID: PMC4151960  PMID: 25181446
5.  Bugs Split to Attack and Gamble to Survive 
PLoS Biology  2014;12(8):e1001929.
doi:10.1371/journal.pbio.1001929
PMCID: PMC4137982  PMID: 25137046
6.  What Are Little Boys and Girls Made of? The Origins of Sexual Dimorphism 
PLoS Biology  2014;12(7):e1001905.
doi:10.1371/journal.pbio.1001905
PMCID: PMC4086712  PMID: 25003370
7.  Stressed Yeast Paint a Picture of Dorian Gray 
PLoS Biology  2014;12(6):e1001885.
doi:10.1371/journal.pbio.1001885
PMCID: PMC4060992  PMID: 24936648
8.  Jocks versus Geeks—the Downside of Genius? 
PLoS Biology  2014;12(5):e1001872.
doi:10.1371/journal.pbio.1001872
PMCID: PMC4035265  PMID: 24866171
9.  Braking Bad: Stopping Translation in Hard Times 
PLoS Biology  2014;12(5):e1001867.
doi:10.1371/journal.pbio.1001867
PMCID: PMC4028182  PMID: 24844695
10.  A Galactic View of Nature's Decontamination Squad 
PLoS Biology  2014;12(4):e1001842.
doi:10.1371/journal.pbio.1001842
PMCID: PMC3995637  PMID: 24756072
11.  The Velvet Underground Emerges 
PLoS Biology  2013;11(12):e1001751.
doi:10.1371/journal.pbio.1001751
PMCID: PMC3876988  PMID: 24391471
12.  Building a Sea Urchin on Shifting Sands 
PLoS Biology  2013;11(10):e1001690.
doi:10.1371/journal.pbio.1001690
PMCID: PMC3812111  PMID: 24204206
13.  Deep Genealogy and the Dilution of Risk 
PLoS Biology  2013;11(9):e1001660.
doi:10.1371/journal.pbio.1001660
PMCID: PMC3775720  PMID: 24068892
14.  Myelination Borrows a Trick from Phage 
PLoS Biology  2013;11(8):e1001626.
doi:10.1371/journal.pbio.1001626
PMCID: PMC3742466  PMID: 23966834
15.  A Read-Through Drug Put through Its Paces 
PLoS Biology  2013;11(6):e1001458.
doi:10.1371/journal.pbio.1001458
PMCID: PMC3692443  PMID: 23824301
16.  Watching Genes Loop the Loop 
PLoS Biology  2013;11(6):e1001592.
doi:10.1371/journal.pbio.1001592
PMCID: PMC3708705  PMID: 23853548
17.  HIV Plays (and Wins) a Game of T Cell Brinkmanship 
PLoS Biology  2013;11(4):e1001521.
doi:10.1371/journal.pbio.1001521
PMCID: PMC3614497  PMID: 23565056
18.  Positive Charges Put the Brakes on Ribosomes 
PLoS Biology  2013;11(3):e1001509.
doi:10.1371/journal.pbio.1001509
PMCID: PMC3595228  PMID: 23554577
19.  Collection Overview: Ten Years of Wonderful Open Access Science 
PLoS Biology  2013;11(10):e1001688.
Announcing our Tenth Anniversary PLOS Biology Collection, Roli Roberts and Jane Alfred introduce the top 10 papers as selected by our Editorial Board Members and the Editorial team.
To mark our tenth Anniversary at PLOS Biology, we are launching a special, celebratory Tenth Anniversary PLOS Biology Collection which showcases 10 specially selected PLOS Biology research articles drawn from a decade of publishing excellent science. It also features newly commissioned articles, including thought-provoking pieces on the Open Access movement (past and present), on article-level metrics, and on the history of the Public Library of Science. Each research article highlighted in the collection is also accompanied by a PLOS Biologue blog post to extend the impact of these remarkable studies to the widest possible audience.
doi:10.1371/journal.pbio.1001688
PMCID: PMC3805470  PMID: 24167446
21.  Large-Scale Modelling of the Divergent Spectrin Repeats in Nesprins: Giant Modular Proteins 
PLoS ONE  2013;8(5):e63633.
Nesprin-1 and nesprin-2 are nuclear envelope (NE) proteins characterized by a common structure of an SR (spectrin repeat) rod domain and a C-terminal transmembrane KASH [Klarsicht–ANC–Syne-homology] domain and display N-terminal actin-binding CH (calponin homology) domains. Mutations in these proteins have been described in Emery-Dreifuss muscular dystrophy and attributed to disruptions of interactions at the NE with nesprins binding partners, lamin A/C and emerin. Evolutionary analysis of the rod domains of the nesprins has shown that they are almost entirely composed of unbroken SR-like structures. We present a bioinformatical approach to accurate definition of the boundaries of each SR by comparison with canonical SR structures, allowing for a large-scale homology modelling of the 74 nesprin-1 and 56 nesprin-2 SRs. The exposed and evolutionary conserved residues identify important pbs for protein-protein interactions that can guide tailored binding experiments. Most importantly, the bioinformatics analyses and the 3D models have been central to the design of selected constructs for protein expression. 1D NMR and CD spectra have been performed of the expressed SRs, showing a folded, stable, high content α-helical structure, typical of SRs. Molecular Dynamics simulations have been performed to study the structural and elastic properties of consecutive SRs, revealing insights in the mechanical properties adopted by these modules in the cell.
doi:10.1371/journal.pone.0063633
PMCID: PMC3646009  PMID: 23671687
22.  Dystrobrevin and dystrophin family gene expression in zebrafish 
Dystrophin/dystrobrevin superfamily proteins play structural and signalling roles at the plasma membrane of many cell types. Defects in them or the associated multiprotein complex cause a range of neuromuscular disorders. Members of the dystrophin branch of the family form heterodimers with members of the dystrobrevin branch, mediated by their coiled-coil domains. To determine which combinations of these proteins might interact during embryonic development, we set out to characterise the gene expression pattern of dystrophin and dystrobrevin family members in zebrafish. γ-dystrobrevin (dtng), a novel dystrobrevin recently identified in fish, is the predominant form of dystrobrevin in embryonic development. Dtng and dmd (dystrophin) have similar spatial and temporal expression patterns in muscle, where transcripts are localized to the ends of differentiated fibres at the somite borders. Dtng is expressed in the notochord while dmd is expressed in the chordo-neural hinge and then in floor plate and hypochord. In addition, dtng is dynamically expressed in rhombomeres 2 and 4-6 of the hindbrain and in the ventral midbrain. α-dystrobrevin (dtna) is expressed widely in the brain with particularly strong expression in the hypothalamus and the telencephalon; drp2 is also expressed widely in the brain. Utrophin expression is found in early pronephros and lateral line development and utrophin and dystrophin are both expressed later in the gut. β-dystrobrevin (dtnb) is expressed in the pronephric duct and widely at low levels. In summary, we find clear instances of co-expression of dystrophin and dystrobrevin family members in muscle, brain and pronephric duct development and many examples of strong and specific expression of members of one family but not the other, an intriguing finding given the presumed heterodimeric state of these molecules.
doi:10.1016/j.modgep.2007.10.004
PMCID: PMC3360968  PMID: 18042440
muscle; zebrafish; notochord; midbrain; rhombomere; gene expression; utrophin; dystrophin; dystrobrevin; drp2; dystrotelin
23.  MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network 
Selective autophagy is a process whereby specific targeted cargo proteins, aggregates, or organelles are sequestered into double-membrane-bound phagophores before fusion with the lysosome for protein degradation. It has been demonstrated that the microtubule network is important for the formation and movement of autophagosomes. Nbr1 is a selective cargo receptor that through its interaction with LC3 recruits ubiquitinated proteins for autophagic degradation. This study demonstrates an interaction between the evolutionarily conserved FW domain of Nbr1 with the microtubule-associated protein MAP1B. Upon autophagy induction, MAP1B localisation is focused into discrete vesicles with Nbr1. This colocalisation is dependent upon an intact microtubule network as depolymerisation by nocodazole treatment abolishes starvation-induced MAP1B recruitment to these vesicles. MAP1B is not recruited to autophagosomes for protein degradation as blockage of lysosomal acidification does not result in significant increased MAP1B protein levels. However, the protein levels of phosphorylated MAP1B are significantly increased upon blockage of autophagic degradation. This is the first evidence that links the ubiquitin receptor Nbr1, which shuttles ubiquitinated proteins to be degraded by autophagy, to the microtubule network.
doi:10.1155/2012/208014
PMCID: PMC3357945  PMID: 22654911
24.  Evolution of a Species-Specific Determinant within Human CRM1 that Regulates the Post-transcriptional Phases of HIV-1 Replication 
PLoS Pathogens  2011;7(11):e1002395.
The human immunodeficiency virus type-1 (HIV-1) Rev protein regulates the nuclear export of intron-containing viral RNAs by recruiting the CRM1 nuclear export receptor. Here, we employed a combination of functional and phylogenetic analyses to identify and characterize a species-specific determinant within human CRM1 (hCRM1) that largely overcomes established defects in murine cells to the post-transcriptional stages of the HIV-1 life cycle. hCRM1 expression in murine cells promotes the cytoplasmic accumulation of intron-containing viral RNAs, resulting in a substantial stimulation of the net production of infectious HIV-1 particles. These stimulatory effects require a novel surface-exposed element within HEAT repeats 9A and 10A, discrete from the binding cleft previously shown to engage Rev's leucine-rich nuclear export signal. Moreover, we show that this element is a unique feature of higher primate CRM1 proteins, and discuss how this sequence has evolved from a non-functional, ancestral sequence.
Author Summary
HIV-1 requires multiple cellular co-factors to replicate, and non-human cells often carry species-specific variations in the genes encoding these co-factors that can prevent efficient replication. Here, the basis for murine cell-specific deficiencies in the late steps of HIV-1 replication is addressed. We show that differences between the mouse and human forms of the essential host protein CRM1, a protein required for the transport of macromolecules from the nucleus to the cytoplasm, underlie this problem. More precisely, murine CRM1, unlike its human counterpart, fails to fully support the function of the HIV-1 Rev protein, a factor necessary to transport viral RNAs to the cytoplasm. Key amino acid differences between the mouse/human CRM1 proteins are identified and computational analyses of divergent animal CRM1 proteins reveal a unique motif in higher primates likely acquired in response to ancient evolutionary pressures. This CRM1 element may represent a novel pathogen interaction site that evolved to evade prior infections, but is now contributing to the susceptibility of humans to HIV-1.
doi:10.1371/journal.ppat.1002395
PMCID: PMC3219727  PMID: 22114565
25.  Heterozygous deletion of a 2-Mb region including the dystroglycan gene in a patient with mild myopathy, facial hypotonia, oral-motor dyspraxia and white matter abnormalities 
Dystroglycan is a protein which binds directly to two proteins defective in muscular dystrophies (dystrophin and laminin α2) and whose own aberrant post-translational modification is the common aetiological route of neuromuscular diseases associated with mutations in genes encoding at least six other proteins (POMT1, POMT2, POMGnT1, LARGE, FKTN and FKRP). It is surprising, therefore, that to our knowledge no mutations of the human dystroglycan gene itself have yet been reported. In this study, we describe a patient with a heterozygous de novo deletion of a ∼2-Mb region of chromosome 3, which includes the dystroglycan gene (DAG1). The patient is a 16-year-old female with learning difficulties, white matter abnormalities, elevated serum creatine kinase, oral-motor dyspraxia and facial hypotonia but minimal clinically significant involvement of other muscles. As these symptoms are a subset of those observed in disorders of dystroglycan glycosylation (muscle–eye–brain disease and Warker–Warburg syndrome), we assess the likely contribution to her phenotype of her heterogosity for a null mutation of DAG1. We also show that the transcriptional compensation observed in the Dag1+/− mouse is not observed in the patient. Although we cannot show that haploinsufficiency of DAG1 is the sole cause of this patient's myopathy and white matter changes, this case serves to constrain our ideas of the severity of the phenotypic consequences of heterozygosity for null DAG1 mutations.
doi:10.1038/ejhg.2010.28
PMCID: PMC2987357  PMID: 20234391
dystroglycan; muscular dystrophy; learning difficulties; white matter; oral-motor dyspraxia

Results 1-25 (36)