HIV-1 matrix protein (MA) is a multifunctional structural protein localized on N terminus of Gag precursor p55. MA participates in HIV-1 assembly as membranotropic part of Gag precursor as well as an individual protei...HIV-1 matrix protein (MA) is a multifunctional structural protein localized on N terminus of Gag precursor p55. MA participates in HIV-1 assembly as membranotropic part of Gag precursor as well as an individual protein spliced from Gag early in infection. MA is found in the nuclei of infected cells and in plasma membrane, the site of virus assembly, in association with viral genome RNA. MA mutated variant M4 which contains two changed amino acids in N-terminal regions is also associated with viral RNA, but it is localized in the nuclear and cytoskeleton fractions but not in the plasma membrane suggesting that the mutant is deprived of membranotropic signal and “sticks” in the nuclei an d cytoskeleton, its previous location sites. These data allow suggesting that MA involved into transmission of viral RNA is transported to plasma membrane by cytoskeleton.展开更多
Objective Findings from the previous studies have suggested a relationship between ectonucleotide pyrophosphatase /phosphodiesterase 1 （ENPP‐1） or plasma cell membrane glycoprotein 1 （PC‐1） gene single nucleotid...Objective Findings from the previous studies have suggested a relationship between ectonucleotide pyrophosphatase /phosphodiesterase 1 （ENPP‐1） or plasma cell membrane glycoprotein 1 （PC‐1） gene single nucleotide polymorphism （K121Q, rs1044498） and genetic susceptibility to obesity. However, such relationship is not reproduced by some currently available studies. In this context, the present study is aimed to quantitatively analyze the association of K121Q variant with obesity in all published case‐control studies in European adult populations. Methods Published literature from PubMed, EMBASE, and ISI web of science databases were retrieved. The studies evaluating the association of ENPP1/PC1 gene K121Q polymorphism with obesity were included, in which sufficient data were presented to calculate the odds ratio （OR） with 95% confidence intervals （CIs）. Results Ten case‐control studies meeting the inclusion criteria identified a total of 24,324 subjects including 11,372 obese and 12,952 control subjects. The meta‐analysis results showed a statistically significant association of K121Q with obesity [OR （95%CI）： 1.25 （1.04‐1.52） P=0.021] under a recessive model of inheritance （QQ vs. KK＋KQ） without heterogeneity or publication bias. Conclusions The results from the present study have indicated that ENPP1/PC1 Q121 variant may increase the risk of obesity and that more well‐designed studies based on a larger population will be required to further evaluate the role of ENPP1/PC1 gene K121Q polymorphism in obesity and other related metabolic syndromes.展开更多
Cotton(Gossypium hirsutum)fibers are elongated single cells that rapidly accumulate cellulose during secondary cell wall(SCW)thickening,which requires cellulose synthase complex(CSC)activity.Here,we describe the CSC-i...Cotton(Gossypium hirsutum)fibers are elongated single cells that rapidly accumulate cellulose during secondary cell wall(SCW)thickening,which requires cellulose synthase complex(CSC)activity.Here,we describe the CSC-interacting factor CASPARIAN STRIP MEMBRANE DOMAIN-LIKE1(GhCASPL1),which contributes to SCW thickening by influencing CSC stability on the plasma membrane.GhCASPL1 is preferentially expressed in fiber cells during SCW biosynthesis and encodes a MARVEL domain protein.The ghcaspl1 ghcaspl2 mutant exhibited reduced plant height and produced mature fibers with fewer natural twists,lower tensile strength,and a thinner SCW compared to the wild type.Similarly,the Arabidopsis(Arabidopsis thaliana)caspl1 caspl2 double mutant showed a lower cellulose content and thinner cell walls in the stem vasculature than the wild type but normal plant morphology.Introducing the cotton gene GhCASPL1 successfully restored the reduced cellulose content of the Arabidopsis caspl1 caspl2 mutant.Detergent treatments,ultracentrifugation assays,and enzymatic assays showed that the CSC in the ghcaspl1 ghcaspl2 double mutant showed reduced membrane binding and decreased enzyme activity compared to the wild type.GhCASPL1 binds strongly to phosphatidic acid(PA),which is present in much higher amounts in thickening fiber cells compared to ovules and leaves.Mutating the PA-binding site in GhCASPL1 resulted in the loss of its colocalization with GhCesA8,and it failed to localize to the plasma membrane.PA may alter membrane structure to facilitate protein–protein interactions,suggesting that GhCASPL1 and PA collaboratively stabilize the CSC.Our findings shed light on CASPL functions and the molecular machinery behind SCW biosynthesis in cotton fibers.展开更多
文摘HIV-1 matrix protein (MA) is a multifunctional structural protein localized on N terminus of Gag precursor p55. MA participates in HIV-1 assembly as membranotropic part of Gag precursor as well as an individual protein spliced from Gag early in infection. MA is found in the nuclei of infected cells and in plasma membrane, the site of virus assembly, in association with viral genome RNA. MA mutated variant M4 which contains two changed amino acids in N-terminal regions is also associated with viral RNA, but it is localized in the nuclear and cytoskeleton fractions but not in the plasma membrane suggesting that the mutant is deprived of membranotropic signal and “sticks” in the nuclei an d cytoskeleton, its previous location sites. These data allow suggesting that MA involved into transmission of viral RNA is transported to plasma membrane by cytoskeleton.
文摘Objective Findings from the previous studies have suggested a relationship between ectonucleotide pyrophosphatase /phosphodiesterase 1 （ENPP‐1） or plasma cell membrane glycoprotein 1 （PC‐1） gene single nucleotide polymorphism （K121Q, rs1044498） and genetic susceptibility to obesity. However, such relationship is not reproduced by some currently available studies. In this context, the present study is aimed to quantitatively analyze the association of K121Q variant with obesity in all published case‐control studies in European adult populations. Methods Published literature from PubMed, EMBASE, and ISI web of science databases were retrieved. The studies evaluating the association of ENPP1/PC1 gene K121Q polymorphism with obesity were included, in which sufficient data were presented to calculate the odds ratio （OR） with 95% confidence intervals （CIs）. Results Ten case‐control studies meeting the inclusion criteria identified a total of 24,324 subjects including 11,372 obese and 12,952 control subjects. The meta‐analysis results showed a statistically significant association of K121Q with obesity [OR （95%CI）： 1.25 （1.04‐1.52） P=0.021] under a recessive model of inheritance （QQ vs. KK＋KQ） without heterogeneity or publication bias. Conclusions The results from the present study have indicated that ENPP1/PC1 Q121 variant may increase the risk of obesity and that more well‐designed studies based on a larger population will be required to further evaluate the role of ENPP1/PC1 gene K121Q polymorphism in obesity and other related metabolic syndromes.
基金supported by the grants from STI 2030—Major Project(2023ZD04069)the Natural Science Foundation of China(32388101 and 32200286)+2 种基金Foundation of Hubei Hongshan Laboratory(2021hszd014)Hubei Provincial Natural Science Foundation of China(2021CFA055)China Postdoctoral Science Foundation(2022TQ0240,2022M722470).
文摘Cotton(Gossypium hirsutum)fibers are elongated single cells that rapidly accumulate cellulose during secondary cell wall(SCW)thickening,which requires cellulose synthase complex(CSC)activity.Here,we describe the CSC-interacting factor CASPARIAN STRIP MEMBRANE DOMAIN-LIKE1(GhCASPL1),which contributes to SCW thickening by influencing CSC stability on the plasma membrane.GhCASPL1 is preferentially expressed in fiber cells during SCW biosynthesis and encodes a MARVEL domain protein.The ghcaspl1 ghcaspl2 mutant exhibited reduced plant height and produced mature fibers with fewer natural twists,lower tensile strength,and a thinner SCW compared to the wild type.Similarly,the Arabidopsis(Arabidopsis thaliana)caspl1 caspl2 double mutant showed a lower cellulose content and thinner cell walls in the stem vasculature than the wild type but normal plant morphology.Introducing the cotton gene GhCASPL1 successfully restored the reduced cellulose content of the Arabidopsis caspl1 caspl2 mutant.Detergent treatments,ultracentrifugation assays,and enzymatic assays showed that the CSC in the ghcaspl1 ghcaspl2 double mutant showed reduced membrane binding and decreased enzyme activity compared to the wild type.GhCASPL1 binds strongly to phosphatidic acid(PA),which is present in much higher amounts in thickening fiber cells compared to ovules and leaves.Mutating the PA-binding site in GhCASPL1 resulted in the loss of its colocalization with GhCesA8,and it failed to localize to the plasma membrane.PA may alter membrane structure to facilitate protein–protein interactions,suggesting that GhCASPL1 and PA collaboratively stabilize the CSC.Our findings shed light on CASPL functions and the molecular machinery behind SCW biosynthesis in cotton fibers.
