The Experts below are selected from a list of 313095 Experts worldwide ranked by ideXlab platform
Liwen Jiang - One of the best experts on this subject based on the ideXlab platform.
-
atbro1 functions in escrt i complex to regulate multivesicular Body Protein sorting
Molecular Plant, 2016Co-Authors: Jinbo Shen, Xiaohong Zhuang, Xiangfeng Wang, Qiong Zhao, Liwen JiangAbstract:Membrane Proteins destined for degradation in eukaryotic cells are tagged by ubiquitin (Ub) for further sorting by the endosomal sorting complex required for transport (ESCRT) machinery into the intraluminal vesicles (ILVs) of multivesicular bodies (MVBs) or prevacuolar compartments (PVCs) for subsequent lysosomal/vacuolar degradation (Henne et al., 2011; Schmidt and Teis, 2012). The ESCRT machinery comprises a cascade of several distinct complexes (ESCRTs -0, -I, -II, and -III, and Vps4 complex).
-
a unique plant escrt component free1 regulates multivesicular Body Protein sorting and plant growth
Current Biology, 2014Co-Authors: Qiong Zhao, Yonglun Zeng, Renzhi Yang, Liwen JiangAbstract:Summary Tight control of membrane Protein homeostasis by selective degradation is crucial for proper cell signaling and multicellular organismal development. Membrane Proteins destined for degradation, such as misfolded Proteins or activated receptors, are usually ubiquitinated and sorted into the intraluminal vesicles (ILVs) of prevacuolar compartments/multivesicular bodies (PVCs/MVBs), which then fuse with vacuoles/lysosomes to deliver their contents to the lumen for degradation by luminal proteases [1]. The formation of ILVs and the sorting of ubiquitinated membrane cargoes into them are facilitated by the endosomal sorting complex required for transport (ESCRT) machinery [2–4]. Plants possess most evolutionarily conserved members of the ESCRT machinery but apparently lack orthologs of ESCRT-0 subunits and the ESCRT-I component Mvb12 [5–8]. Here, we identified a unique plant ESCRT component called FYVE domain Protein required for endosomal sorting 1 (FREE1). FREE1 binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin and specifically interacts with Vps23 via PTAP-like tetrapeptide motifs to be incorporated into the ESCRT-I complex. Arabidopsis free1 mutant is seedling lethal and defective in the formation of ILVs in MVBs. Consequently, endocytosed plasma membrane (PM) Proteins destined for degradation, such as the auxin efflux carrier PIN2 [9, 10], cannot reach the lumen of the vacuole and mislocalize to the tonoplast. Collectively, our findings provide the first functional characterization of a plant FYVE domain Protein, which is essential for plant growth via its role as a unique evolutionary ESCRT component for MVB biogenesis and vacuolar sorting of membrane Proteins.
-
a unique plant escrt component free1 regulates multivesicular Body Protein sorting and plant growth
Current Biology, 2014Co-Authors: Qiong Zhao, Yonglun Zeng, Renzhi Yang, Liwen JiangAbstract:Summary Tight control of membrane Protein homeostasis by selective degradation is crucial for proper cell signaling and multicellular organismal development. Membrane Proteins destined for degradation, such as misfolded Proteins or activated receptors, are usually ubiquitinated and sorted into the intraluminal vesicles (ILVs) of prevacuolar compartments/multivesicular bodies (PVCs/MVBs), which then fuse with vacuoles/lysosomes to deliver their contents to the lumen for degradation by luminal proteases [1]. The formation of ILVs and the sorting of ubiquitinated membrane cargoes into them are facilitated by the endosomal sorting complex required for transport (ESCRT) machinery [2–4]. Plants possess most evolutionarily conserved members of the ESCRT machinery but apparently lack orthologs of ESCRT-0 subunits and the ESCRT-I component Mvb12 [5–8]. Here, we identified a unique plant ESCRT component called FYVE domain Protein required for endosomal sorting 1 (FREE1). FREE1 binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin and specifically interacts with Vps23 via PTAP-like tetrapeptide motifs to be incorporated into the ESCRT-I complex. Arabidopsis free1 mutant is seedling lethal and defective in the formation of ILVs in MVBs. Consequently, endocytosed plasma membrane (PM) Proteins destined for degradation, such as the auxin efflux carrier PIN2 [9, 10], cannot reach the lumen of the vacuole and mislocalize to the tonoplast. Collectively, our findings provide the first functional characterization of a plant FYVE domain Protein, which is essential for plant growth via its role as a unique evolutionary ESCRT component for MVB biogenesis and vacuolar sorting of membrane Proteins.
Qiong Zhao - One of the best experts on this subject based on the ideXlab platform.
-
atbro1 functions in escrt i complex to regulate multivesicular Body Protein sorting
Molecular Plant, 2016Co-Authors: Jinbo Shen, Xiaohong Zhuang, Xiangfeng Wang, Qiong Zhao, Liwen JiangAbstract:Membrane Proteins destined for degradation in eukaryotic cells are tagged by ubiquitin (Ub) for further sorting by the endosomal sorting complex required for transport (ESCRT) machinery into the intraluminal vesicles (ILVs) of multivesicular bodies (MVBs) or prevacuolar compartments (PVCs) for subsequent lysosomal/vacuolar degradation (Henne et al., 2011; Schmidt and Teis, 2012). The ESCRT machinery comprises a cascade of several distinct complexes (ESCRTs -0, -I, -II, and -III, and Vps4 complex).
-
a unique plant escrt component free1 regulates multivesicular Body Protein sorting and plant growth
Current Biology, 2014Co-Authors: Qiong Zhao, Yonglun Zeng, Renzhi Yang, Liwen JiangAbstract:Summary Tight control of membrane Protein homeostasis by selective degradation is crucial for proper cell signaling and multicellular organismal development. Membrane Proteins destined for degradation, such as misfolded Proteins or activated receptors, are usually ubiquitinated and sorted into the intraluminal vesicles (ILVs) of prevacuolar compartments/multivesicular bodies (PVCs/MVBs), which then fuse with vacuoles/lysosomes to deliver their contents to the lumen for degradation by luminal proteases [1]. The formation of ILVs and the sorting of ubiquitinated membrane cargoes into them are facilitated by the endosomal sorting complex required for transport (ESCRT) machinery [2–4]. Plants possess most evolutionarily conserved members of the ESCRT machinery but apparently lack orthologs of ESCRT-0 subunits and the ESCRT-I component Mvb12 [5–8]. Here, we identified a unique plant ESCRT component called FYVE domain Protein required for endosomal sorting 1 (FREE1). FREE1 binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin and specifically interacts with Vps23 via PTAP-like tetrapeptide motifs to be incorporated into the ESCRT-I complex. Arabidopsis free1 mutant is seedling lethal and defective in the formation of ILVs in MVBs. Consequently, endocytosed plasma membrane (PM) Proteins destined for degradation, such as the auxin efflux carrier PIN2 [9, 10], cannot reach the lumen of the vacuole and mislocalize to the tonoplast. Collectively, our findings provide the first functional characterization of a plant FYVE domain Protein, which is essential for plant growth via its role as a unique evolutionary ESCRT component for MVB biogenesis and vacuolar sorting of membrane Proteins.
-
a unique plant escrt component free1 regulates multivesicular Body Protein sorting and plant growth
Current Biology, 2014Co-Authors: Qiong Zhao, Yonglun Zeng, Renzhi Yang, Liwen JiangAbstract:Summary Tight control of membrane Protein homeostasis by selective degradation is crucial for proper cell signaling and multicellular organismal development. Membrane Proteins destined for degradation, such as misfolded Proteins or activated receptors, are usually ubiquitinated and sorted into the intraluminal vesicles (ILVs) of prevacuolar compartments/multivesicular bodies (PVCs/MVBs), which then fuse with vacuoles/lysosomes to deliver their contents to the lumen for degradation by luminal proteases [1]. The formation of ILVs and the sorting of ubiquitinated membrane cargoes into them are facilitated by the endosomal sorting complex required for transport (ESCRT) machinery [2–4]. Plants possess most evolutionarily conserved members of the ESCRT machinery but apparently lack orthologs of ESCRT-0 subunits and the ESCRT-I component Mvb12 [5–8]. Here, we identified a unique plant ESCRT component called FYVE domain Protein required for endosomal sorting 1 (FREE1). FREE1 binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin and specifically interacts with Vps23 via PTAP-like tetrapeptide motifs to be incorporated into the ESCRT-I complex. Arabidopsis free1 mutant is seedling lethal and defective in the formation of ILVs in MVBs. Consequently, endocytosed plasma membrane (PM) Proteins destined for degradation, such as the auxin efflux carrier PIN2 [9, 10], cannot reach the lumen of the vacuole and mislocalize to the tonoplast. Collectively, our findings provide the first functional characterization of a plant FYVE domain Protein, which is essential for plant growth via its role as a unique evolutionary ESCRT component for MVB biogenesis and vacuolar sorting of membrane Proteins.
Daniel R Moore - One of the best experts on this subject based on the ideXlab platform.
-
Protein to maximize whole Body anabolism in resistance trained females after exercise
Medicine and Science in Sports and Exercise, 2019Co-Authors: Julia M Malowany, Kimberly A Volterman, Daniel W D West, Eric Williamson, Sidney Abou Sawan, Michael Mazzulla, Daniel R MooreAbstract:ABSTRACTIntroductionCurrent athlete-specific Protein recommendations are based almost exclusively on research in males.PurposeUsing the minimally invasive indicator amino acid oxidation technique, we determined the daily Protein intake that maximizes whole-Body Protein synthesis (PS) and net Protein
-
nutritionally non essential amino acids are dispensable for whole Body Protein synthesis after exercise in endurance athletes with an adequate essential amino acid intake
Amino Acids, 2018Co-Authors: Hiroyuki Kato, Katsuya Suzuki, Kimberly A Volterman, Daniel W D West, Daniel R MooreAbstract:The increased Protein requirement of endurance athletes may be related to the need to replace exercise-induced oxidative losses, especially of the branched-chain amino acids (BCAA). However, it is unknown if non-essential amino acids (NEAA) influence the requirement for essential amino acids (EAA) during post-exercise recovery. Seven endurance-trained males ran 20 km prior to consuming [13C]phenylalanine, sufficient energy, and: (1) deficient Protein (BASE); (2) BASE supplemented with sufficient BCAA (BCAAsup); (3) an equivalent EAA intake as BCAA (LowEAA), and; (4) sufficient EAA intake (HighEAA). [13C]Phenylalanine oxidation (the reciprocal of Protein synthesis) for BCAAsup and HighEAA (0.54 ± 0.15, 0.49 ± 0.11 µmol kg−1 h−1; Mean ± SD) were significantly lower than BASE (0.74 ± 0.14 µmol kg−1 h−1; P < 0.01 for both) and LowEAA (0.70 ± 0.11 µmol kg−1 h−1; P < 0.05 and 0.01, respectively). Our results suggest that exogenous NEAA are dispensable for whole-Body Protein synthesis during recovery from endurance exercise provided sufficient EAA are consumed. Endurance athletes who may be at risk of not meeting their elevated Protein requirements should prioritize the intake of EAA-enriched foods and/or supplements.
-
daytime pattern of post exercise Protein intake affects whole Body Protein turnover in resistance trained males
Nutrition & Metabolism, 2012Co-Authors: Daniel R Moore, Jose L Areta, Vernon G Coffey, Trent Stellingwerff, Stuart M Phillips, Louise M Burke, Marilyn Cleroux, Jeanphilippe GodinAbstract:Background The pattern of Protein intake following exercise may impact whole-Body Protein turnover and net Protein retention. We determined the effects of different Protein feeding strategies on Protein metabolism in resistance-trained young men.
-
daytime pattern of post exercise Protein intake affects whole Body Protein turnover in resistance trained males
Faculty of Health, 2012Co-Authors: Daniel R Moore, Jose L Areta, Vernon G Coffey, Trent Stellingwerff, Stuart M Phillips, Louise M Burke, Marilyn Cleroux, Jeanphilippe GodinAbstract:Background The pattern of Protein intake following exercise may impact whole-Body Protein turnover and net Protein retention. We determined the effects of different Protein feeding strategies on Protein metabolism in resistance-trained young men. Methods: Participants were randomly assigned to ingest either 80g of whey Protein as 8x10g every 1.5h (PULSE; n=8), 4x20g every 3h (intermediate, INT; n=7), or 2x40g every 6h (BOLUS; n=8) after an acute bout of bilateral knee extension exercise (4x10 repetitions at 80% maximal strength). Whole-Body Protein turnover (Q), synthesis (S), breakdown (B), and net balance (NB) were measured throughout 12h of recovery by a bolus ingestion of [ 15N]glycine with urinary [15N]ammonia enrichment as the collected end-product. Results PULSE Q rates were greater than BOLUS (?19%, P<0.05) with a trend towards being greater than INT (?9%, P=0.08). Rates of S were 32% and 19% greater and rates of B were 51% and 57% greater for PULSE as compared to INT and BOLUS, respectively (P<0.05), with no difference between INT and BOLUS. There were no statistical differences in NB between groups (P=0.23); however, magnitude-based inferential statistics revealed likely small (mean effect90%CI; 0.590.87) and moderate (0.800.91) increases in NB for PULSE and INT compared to BOLUS and possible small increase (0.421.00) for INT vs. PULSE. Conclusion We conclude that the pattern of ingested Protein, and not only the total daily amount, can impact whole-Body Protein metabolism. Individuals aiming to maximize NB would likely benefit from repeated ingestion of moderate amounts of Protein (?20g) at regular intervals (?3h) throughout the day.
Robert R Wolfe - One of the best experts on this subject based on the ideXlab platform.
-
anabolic response to essential amino acid plus whey Protein composition is greater than whey Protein alone in young healthy adults
Journal of The International Society of Sports Nutrition, 2020Co-Authors: Sanghee Park, Scott Schutzler, Arny A. Ferrando, Gohar Azhar, David D Church, Robert R WolfeAbstract:We have determined the acute response of Protein kinetics to one or two servings (6.3 g and 12.6 g) of a proprietary composition containing free-form essential amino acids (EAA) (3.2 g EAA per serving) and whey Protein (2.4 g per serving), as well as the response to consumption of a popular whey-based Protein supplement (Gatorade Recover) (17 g; 12.6 g Protein). Whole-Body rates of Protein synthesis, breakdown and net balance (taken to be the anabolic response) were determined using primed-constant infusions of 2H5-phenylalnine and 2H2-tyrosine. Muscle Protein fractional synthetic rate (FSR) was also determined with the 2H5-phenylalanine tracer. Plasma EAA levels increased following consumption of all beverages, with the greatest response in the high-dose EAA/Protein composition. Similarly, the increase in net balance between whole-Body Protein synthesis and breakdown was greatest following consumption of the high-dose EAA/Protein composition, while the low-dose EAA/Protein composition and Gatorade Recover induced similar increases in net balance. When the net balance response was normalized for the total amount of product given, the high- and low-dose EAA/Protein beverages were approximately 6- and 3-fold more anabolic than the Gatorade Recover, respectively. The greater anabolic response to the EAA/Protein composition was due to greater increases in whole-Body Protein synthesis with both doses, and a markedly greater suppression of whole-Body Protein breakdown in the high-dose group. Muscle Protein FSR after beverage consumption reflected changes in whole-Body Protein synthesis, with the larger EAA/Protein dose significantly increasing FSR. We conclude that a composition of a balanced EAA formulation combined with whey Protein is highly anabolic as compared to a whey Protein-based recovery product, and that the response is dose-dependent. ClinicalTrials.gov Identifier: NCT03502941. This trial was registered on April 19, 2018.
-
advances in stable isotope tracer methodology part 2 new thoughts about an old method measurement of whole Body Protein synthesis and breakdown in the fed state
Journal of Investigative Medicine, 2020Co-Authors: Robert R Wolfe, Il-young Kim, Arny A. Ferrando, Sanghee Park, Paul J MoughanAbstract:Whole-Body Protein turnover (Protein synthesis, breakdown, and net balance) model enables quantification of the response to a variety of circumstances, including the response to meal feeding. In the fed state, the whole-Body Protein turnover model requires taking account of the contribution of absorbed tracee to the observed total appearance of tracee in the peripheral blood (exogenous appearance, RaEXO). There are different approaches to estimating RaEXO. The use of an intrinsically labeled dietary Protein is based on the overriding assumption that the appearance in the peripheral circulation of a tracer amino acid incorporated into a dietary Protein is exactly proportional to the appearance of absorbed tracee. The bioavailability approach is based on the true ileal digestibility of the dietary Protein and the irreversible loss of the tracee in the splanchnic bed via hydroxylation of the tracee (phenylalanine). Finally, RaEXO can be estimated as the increase above the basal rate of appearance of the tracee using traditional tracer dilution methodology. In this paper, we discuss the pros and cons of each approach and conclude that the bioavailability method is the least likely to introduce systematic errors and is therefore the preferable approach.
-
consumption of a specially formulated mixture of essential amino acids promotes gain in whole Body Protein to a greater extent than a complete meal replacement in older women with heart failure
Nutrients, 2019Co-Authors: Il-young Kim, Scott Schutzler, Arny A. Ferrando, Sanghee Park, Ellen T H C Smeets, Gohar Azhar, Jeanne Y Wei, Robert R WolfeAbstract:Heart failure in older individuals is normally associated with a high Body mass index and relatively low lean Body mass due to, in part, a resistance to the normal anabolic effect of dietary Protein. In this study we have investigated the hypothesis that consumption of a specially-formulated composition of essential amino acids (HiEAAs) can overcome anabolic resistance in individuals with heart failure and stimulate the net gain of Body Protein to a greater extent than a commercially popular Protein-based meal replacement beverage with greater caloric but lower essential amino acid (EAA) content (LoEAA). A randomized cross-over design was used. Protein kinetics were determined using primed continuous infusions of L-(2H5)phenylalanine and L-(2H2)tyrosine in the basal state and for four hours following consumption of either beverage. Both beverages induced positive net Protein balance (i.e., anabolic response). However, the anabolic response was more than two times greater with the HiEAA than the LoEAA (p < 0.001), largely through a greater suppression of Protein breakdown (p < 0.001). Net Protein accretion (g) was also greater in the HiEAA when data were normalized for either amino acid or caloric content (p < 0.001). We conclude that a properly formulated EAA mixture can elicit a greater anabolic response in individuals with heart failure than a Protein-based meal replacement. Since heart failure is often associated with obesity, the minimal caloric value of the HiEAA formulation is advantageous.
-
phenylalanine isotope pulse method to measure effect of sepsis on Protein breakdown and membrane transport in the pig
American Journal of Physiology-endocrinology and Metabolism, 2017Co-Authors: Gabriella Ten A M Have, Robert R Wolfe, Marielle P K J Engelen, Nicolaas E. P. DeutzAbstract:The primed-continuous (PC) phenylalanine (Phe) stable isotope infusion methodology is often used as a proxy for measuring whole Body Protein breakdown (WbPB) in sepsis. It is unclear if WbPB data o...
-
Quantity of dietary Protein intake, but not pattern of intake, affects net Protein balance primarily through differences in Protein synthesis in older adults
American journal of physiology. Endocrinology and metabolism, 2014Co-Authors: Il-young Kim, Robert R Wolfe, Nicolaas E. P. Deutz, Scott Schutzler, Amy M. Schrader, Horace J. Spencer, Patrick Kortebein, Arny A. FerrandoAbstract:To examine whole Body Protein turnover and muscle Protein fractional synthesis rate (MPS) following ingestions of Protein in mixed meals at two doses of Protein and two intake patterns, 20 healthy ...
Yonglun Zeng - One of the best experts on this subject based on the ideXlab platform.
-
a unique plant escrt component free1 regulates multivesicular Body Protein sorting and plant growth
Current Biology, 2014Co-Authors: Qiong Zhao, Yonglun Zeng, Renzhi Yang, Liwen JiangAbstract:Summary Tight control of membrane Protein homeostasis by selective degradation is crucial for proper cell signaling and multicellular organismal development. Membrane Proteins destined for degradation, such as misfolded Proteins or activated receptors, are usually ubiquitinated and sorted into the intraluminal vesicles (ILVs) of prevacuolar compartments/multivesicular bodies (PVCs/MVBs), which then fuse with vacuoles/lysosomes to deliver their contents to the lumen for degradation by luminal proteases [1]. The formation of ILVs and the sorting of ubiquitinated membrane cargoes into them are facilitated by the endosomal sorting complex required for transport (ESCRT) machinery [2–4]. Plants possess most evolutionarily conserved members of the ESCRT machinery but apparently lack orthologs of ESCRT-0 subunits and the ESCRT-I component Mvb12 [5–8]. Here, we identified a unique plant ESCRT component called FYVE domain Protein required for endosomal sorting 1 (FREE1). FREE1 binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin and specifically interacts with Vps23 via PTAP-like tetrapeptide motifs to be incorporated into the ESCRT-I complex. Arabidopsis free1 mutant is seedling lethal and defective in the formation of ILVs in MVBs. Consequently, endocytosed plasma membrane (PM) Proteins destined for degradation, such as the auxin efflux carrier PIN2 [9, 10], cannot reach the lumen of the vacuole and mislocalize to the tonoplast. Collectively, our findings provide the first functional characterization of a plant FYVE domain Protein, which is essential for plant growth via its role as a unique evolutionary ESCRT component for MVB biogenesis and vacuolar sorting of membrane Proteins.
-
a unique plant escrt component free1 regulates multivesicular Body Protein sorting and plant growth
Current Biology, 2014Co-Authors: Qiong Zhao, Yonglun Zeng, Renzhi Yang, Liwen JiangAbstract:Summary Tight control of membrane Protein homeostasis by selective degradation is crucial for proper cell signaling and multicellular organismal development. Membrane Proteins destined for degradation, such as misfolded Proteins or activated receptors, are usually ubiquitinated and sorted into the intraluminal vesicles (ILVs) of prevacuolar compartments/multivesicular bodies (PVCs/MVBs), which then fuse with vacuoles/lysosomes to deliver their contents to the lumen for degradation by luminal proteases [1]. The formation of ILVs and the sorting of ubiquitinated membrane cargoes into them are facilitated by the endosomal sorting complex required for transport (ESCRT) machinery [2–4]. Plants possess most evolutionarily conserved members of the ESCRT machinery but apparently lack orthologs of ESCRT-0 subunits and the ESCRT-I component Mvb12 [5–8]. Here, we identified a unique plant ESCRT component called FYVE domain Protein required for endosomal sorting 1 (FREE1). FREE1 binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin and specifically interacts with Vps23 via PTAP-like tetrapeptide motifs to be incorporated into the ESCRT-I complex. Arabidopsis free1 mutant is seedling lethal and defective in the formation of ILVs in MVBs. Consequently, endocytosed plasma membrane (PM) Proteins destined for degradation, such as the auxin efflux carrier PIN2 [9, 10], cannot reach the lumen of the vacuole and mislocalize to the tonoplast. Collectively, our findings provide the first functional characterization of a plant FYVE domain Protein, which is essential for plant growth via its role as a unique evolutionary ESCRT component for MVB biogenesis and vacuolar sorting of membrane Proteins.