150 research outputs found

    Behavioural Ecology Traits of Elusive Deep-Diver Whales Unravel a Complex Social Structure Influenced by Female Philopatry and Defence Polygyny

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    Knowledge of the role of individual associations has provided an insightful understanding of the structures of animal societies, especially in highly social mammals such as primates. Yet, this is unbalanced towards marine mammals, particularly to beaked whales, due to their elusive nature. In addition, information on the fundamental drivers of the social structure of these deep-diving animals is still scarce. Here, the hypothesis of female defence polygyny was tested in Blainville’s beaked whales (Mesoplodon densirostris) and discussed within the context of marine and terrestrial organisms displaying similar patterns, by (i) estimating residency times to obtain information on the movements into and out of the area, (ii) analysing social networks to assess individual association metrics, (iii) measuring the strength of the associations to assess the existence of preferred or avoided relationships among individuals, and (iv) modelling different social structures to address temporal patterns in social relationships. Using a 9-year photographic dataset derived from the pelagic habitat, individual associations were inferred based on likelihood techniques. This approach allowed to infer on the species’ social structure in relation to age class, sex, residency status, and spatio-temporal patterns, which can be a good practice to be applied for other taxa. Heterogeneity in capture probability and residency times was observed between age-sex classes, with adult females exhibiting long-term site fidelity. This suggests different habitat roles and spatial structuring within this social organisation. Strong and long dyadic associations occurred between adult females and immatures, contrarily to between males, and the best-fitting models of the temporal patterns suggested long-lasting and temporary associations. The present findings unravel a complex social structure stratified by age-sex class and influenced by female philopatry and defence polygyny, like an unimale group mating system, which varies from other beaked whales but is similar to some birds, pinnipeds, or non-human primates.FUNDING: The Oceanic Observatory of Madeira and the Portuguese Foundation for Science and Technology (FCT) throughout the strategic projects M1420-01-0142-FEDER-000001 and UIDB/04292/2020, respectively. AB was supported by a MARE grant throughout the project UIDB/04292/2020, AD by ARDITI throughout the project M1420-09-5369-FSE-000002, RF by the FCT grant SFRH/BD/147225/2019, AS by the FCT grant SFRH/BD/141609/2018, MF by the MAC2/1.1a/385 in the framework of INTERTAGUA (MAC INTERREG 2014-2020), and FA by the FCT project UIDP/04292/2020 granted to MARE.info:eu-repo/semantics/publishedVersio

    Asymmetric Requirements for a Rab Gtpase and Snare Proteins in Fusion of Copii Vesicles with Acceptor Membranes

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    Soluble NSF attachment protein receptor (SNARE) proteins are essential for membrane fusion in transport between the yeast ER and Golgi compartments. Subcellular fractionation experiments demonstrate that the ER/Golgi SNAREs Bos1p, Sec22p, Bet1p, Sed5p, and the Rab protein, Ypt1p, are distributed similarly but localize primarily with Golgi membranes. All of these SNARE proteins are efficiently packaged into COPII vesicles and suggest a dynamic cycling of SNARE machinery between ER and Golgi compartments. Ypt1p is not efficiently packaged into vesicles under these conditions. To determine in which membranes protein function is required, temperature-sensitive alleles of BOS1, BET1, SED5, SLY1, and YPT1 that prevent ER/Golgi transport in vitro at restrictive temperatures were used to selectively inactivate these gene products on vesicles or on Golgi membranes. Vesicles bearing mutations in Bet1p or Bos1p inhibit fusion with wild-type acceptor membranes, but acceptor membranes containing these mutations are fully functional. In contrast, vesicles bearing mutations in Sed5p, Sly1p, or Ypt1p are functional, whereas acceptor membranes containing these mutations block fusion. Thus, this set of SNARE proteins is symmetrically distributed between vesicle and acceptor compartments, but they function asymmetrically such that Bet1p and Bos1p are required on vesicles and Sed5p activity is required on acceptor membranes. We propose the asymmetry in SNARE protein function is maintained by an asymmetric distribution and requirement for the Ypt1p GTPase in this fusion event. When a transmembrane-anchored form of Ypt1p is used to restrict this GTPase to the acceptor compartment, vesicles depleted of Ypt1p remain competent for fusion

    Comparative analysis of involvement of UGT1 and UGT2 splice variants of UDP-galactose transporter in glycosylation of macromolecules in MDCK and CHO cell lines

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    Nucleotide sugar transporters deliver nucleotide sugars into the Golgi apparatus and endoplasmic reticulum. This study aimed to further characterize mammalian UDP-galactose transporter (UGT) in MDCK and CHO cell lines. MDCK-RCAr and CHO-Lec8 mutant cell lines are defective in UGT transporter, although they exhibit some level of galactosylation. Previously, only single forms of UGT were identified in both cell lines, UGT1 in MDCK cells and UGT2 in CHO cells. We have identified the second UGT splice variants in CHO (UGT1) and MDCK (UGT2) cells. Compared to UGT1, UGT2 is more abundant in nearly all examined mammalian tissues and cell lines, but MDCK cells exhibit different relative distribution of both splice variants. Complementation analysis demonstrated that both UGT splice variants are necessary for N- and O-glycosylation of proteins. Both mutant cell lines produce chondroitin-4-sulfate at only a slightly lower level compared to wild-type cells. This defect is corrected by overexpression of both UGT splice variants. MDCK-RCAr mutant cells do not produce keratan sulfate and this effect is not corrected by either UGT splice variant, overexpressed either singly or in combination. Here we demonstrate that both UGT splice variants are important for glycosylation of proteins. In contrast to MDCK cells, MDCK-RCAr mutant cells may possess an additional defect within the keratan sulfate biosynthesis pathway

    Carbohydrates and glycosylation

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    Secreted proteins defy the expression level–evolutionary rate anticorrelation

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    The rates of evolution of the proteins of any organism vary across orders of magnitude. A primary factor influencing rates of protein evolution is expression. A strong negative correlation between expression levels and evolutionary rates (the so-called E–R anticorrelation) has been observed in virtually all studied organisms. This effect is currently attributed to the abundance-dependent fitness costs of misfolding and unspecific protein–protein interactions, among other factors. Secreted proteins are folded in the endoplasmic reticulum, a compartment where chaperones, folding catalysts, and stringent quality control mechanisms promote their correct folding and may reduce the fitness costs of misfolding. In addition, confinement of secreted proteins to the extracellular space may reduce misinteractions and their deleterious effects. We hypothesize that each of these factors (the secretory pathway quality control and extracellular location) may reduce the strength of the E–R anticorrelation. Indeed, here we show that among human proteins that are secreted to the extracellular space, rates of evolution do not correlate with protein abundances. This trend is robust to controlling for several potentially confounding factors and is also observed when analyzing protein abundance data for 6 human tissues. In addition, analysis of mRNA abundance data for 32 human tissues shows that the E–R correlation is always less negative, and sometimes nonsignificant, in secreted proteins. Similar observations were made in Caenorhabditis elegans and in Escherichia coli, and to a lesser extent in Drosophila melanogaster, Saccharomyces cerevisiae and Arabidopsis thaliana. Our observations contribute to understand the causes of the E–R anticorrelation

    N‐glycoproteins exhibit a positive expression level–evolutionary rate correlation

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    The different proteins of any proteome evolve at enormously different rates. One of the primary factors influencing rates of protein evolution is expression level, with highly expressed proteins tending to evolve at slow rates. This phenomenon, known as the expression level–evolutionary rate (E–R) anticorrelation, has been attributed to the abundance‐dependent deleterious effects of misfolding or misinteraction. We have recently shown that secreted proteins either lack an E–R anticorrelation or exhibit a significantly reduced E–R anticorrelation. This effect may be due to the strict quality control to which secreted proteins are subject in the endoplasmic reticulum (which is expected to reduce the rate of misfolding and its deleterious effects) or to their extracellular location (expected to reduce the rate of misinteraction and its deleterious effects). Among secreted proteins, N‐glycosylated ones are under particularly strong quality control. Here, we investigate how N‐linked glycosylation affects the E–R anticorrelation. Strikingly, we observe a positive E–R correlation among N‐glycosylated proteins. That is, N‐glycoproteins that are highly expressed evolve at faster rates than lowly expressed N‐glycoproteins, in contrast to what is observed among intracellular proteins
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