Product Information

Total Page：16

File Type：pdf, Size：1020Kb

Product information VPS25, 1-176aa Human, His-tagged, Recombinant, E.coli Cat. No. IBATGP1447 Full name: Vacuolar protein-sorting-associated protein 25 NCBI Accession No.: NP_115729 Synonyms: DERP9, EAP20, FAP20 Description: VPS25, also known as vacuolar protein-sorting-associated protein 25, consists of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may play a role in transcription regulation, possibly via its interaction with ELL. Recombinant human VPS25 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Form: Liquid. 20mM Tris-HCl buffer (pH8.0) containing 20% glycerol 0.1M Nacl Molecular Weight: 23.3 kDa(200aa), confirmed by MALDI-TOF Purity: > 85% by SDS - PAGE Concentration: 0.5 mg/ml (determined by Bradford assay) 15% SDS-PAGE (3ug) Sequences of amino acids: MGSSHHHHHH SSGLVPRGSH MGSHMAMSFE WPWQYRFPPF FTLQPNVDTR QKQLAAWCSL VLSFCRLHKQ SSMTVMEAQE SPLFNNVKLQ RKLPVESIQI VLEELRKKGN LEWLDKSKSS FLIMWRRPEE WGKLIYQWVS RSGQNNSVFT LYELTNGEDT EDEEFHGLDE ATLLRALQAL QQEHKAEIIT VSDGRGVKFF General references: Bailey,S.D. et al. (2010) Diabetes Care 33 (10), 2250-2253 Talmud,P.J. et al. (2009) Am. J. Hum. Genet. 85 (5), 628-642 Storage: Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles. For research use only. This product is not intended or approved for human, diagnostics or veterinary use. Immuno-Biological Laboratories, Inc. (IBL-America) 8201 Central Ave. NE, Suite P, Minneapolis, Minnesota 55432, USA Phone: (888) 523-1246 Fax.: (763) 780-2988 Email: [email protected] Web: www.ibl-america.com.

Copy Link

Recommended publications

Genetic and Genomic Analysis of Hyperlipidemia, Obesity and Diabetes Using (C57BL/6J × TALLYHO/Jngj) F2 Mice
University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Nutrition Publications and Other Works Nutrition 12-19-2010 Genetic and genomic analysis of hyperlipidemia, obesity and diabetes using (C57BL/6J × TALLYHO/JngJ) F2 mice Taryn P. Stewart Marshall University Hyoung Y. Kim University of Tennessee - Knoxville, [email protected] Arnold M. Saxton University of Tennessee - Knoxville, [email protected] Jung H. Kim Marshall University Follow this and additional works at: https://trace.tennessee.edu/utk_nutrpubs Part of the Animal Sciences Commons, and the Nutrition Commons Recommended Citation BMC Genomics 2010, 11:713 doi:10.1186/1471-2164-11-713 This Article is brought to you for free and open access by the Nutrition at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Nutrition Publications and Other Works by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. Stewart et al. BMC Genomics 2010, 11:713 http://www.biomedcentral.com/1471-2164/11/713 RESEARCH ARTICLE Open Access Genetic and genomic analysis of hyperlipidemia, obesity and diabetes using (C57BL/6J × TALLYHO/JngJ) F2 mice Taryn P Stewart1, Hyoung Yon Kim2, Arnold M Saxton3, Jung Han Kim1* Abstract Background: Type 2 diabetes (T2D) is the most common form of diabetes in humans and is closely associated with dyslipidemia and obesity that magnifies the mortality and morbidity related to T2D. The genetic contribution to human T2D and related metabolic disorders is evident, and mostly follows polygenic inheritance. The TALLYHO/ JngJ (TH) mice are a polygenic model for T2D characterized by obesity, hyperinsulinemia, impaired glucose uptake and tolerance, hyperlipidemia, and hyperglycemia.
[Show full text]
Why Cells and Viruses Cannot Survive Without an ESCRT
cells Review Why Cells and Viruses Cannot Survive without an ESCRT Arianna Calistri * , Alberto Reale, Giorgio Palù and Cristina Parolin Department of Molecular Medicine, University of Padua, 35121 Padua, Italy; [email protected] (A.R.); [email protected] (G.P.); [email protected] (C.P.) * Correspondence: [email protected] Abstract: Intracellular organelles enwrapped in membranes along with a complex network of vesicles trafﬁcking in, out and inside the cellular environment are one of the main features of eukaryotic cells. Given their central role in cell life, compartmentalization and mechanisms allowing their maintenance despite continuous crosstalk among different organelles have been deeply investigated over the past years. Here, we review the multiple functions exerted by the endosomal sorting complex required for transport (ESCRT) machinery in driving membrane remodeling and ﬁssion, as well as in repairing physiological and pathological membrane damages. In this way, ESCRT machinery enables different fundamental cellular processes, such as cell cytokinesis, biogenesis of organelles and vesicles, maintenance of nuclear–cytoplasmic compartmentalization, endolysosomal activity. Furthermore, we discuss some examples of how viruses, as obligate intracellular parasites, have evolved to hijack the ESCRT machinery or part of it to execute/optimize their replication cycle/infection. A special emphasis is given to the herpes simplex virus type 1 (HSV-1) interaction with the ESCRT proteins, considering the peculiarities of this interplay and the need for HSV-1 to cross both the nuclear-cytoplasmic and the cytoplasmic-extracellular environment compartmentalization to egress from infected cells. Citation: Calistri, A.; Reale, A.; Palù, Keywords: ESCRT; viruses; cellular membranes; extracellular vesicles; HSV-1 G.; Parolin, C.
[Show full text]
Anti-VPS25 Monoclonal Antibody, Clone T3 (DCABH-13967) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-VPS25 monoclonal antibody, clone T3 (DCABH-13967) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description VPS25, VPS36 (MIM 610903), and SNF8 (MIM 610904) form ESCRT-II (endosomal sorting complex required for transport II), a complex involved in endocytosis of ubiquitinated membrane proteins. VPS25, VPS36, and SNF8 are also associated in a multiprotein complex with RNA polymerase II elongation factor (ELL; MIM 600284) (Slagsvold et al., 2005 [PubMed 15755741]; Kamura et al., 2001 [PubMed 11278625]). Immunogen VPS25 (AAH06282.1, 1 a.a. ~ 176 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. Isotype IgG1 Source/Host Mouse Species Reactivity Human Clone T3 Conjugate Unconjugated Applications Western Blot (Cell lysate); Western Blot (Recombinant protein); ELISA Sequence Similarities MAMSFEWPWQYRFPPFFTLQPNVDTRQKQLAAWCSLVLSFCRLHKQSSMTVMEAQESPLFNN VKLQRKLPVESIQIVLEELRKKGNLEWLDKSKSSFLIMWRRPEEWGKLIYQWVSRSGQNNSVFT LYELTNGEDTEDEEFHGLDEATLLRALQALQQEHKAEIITVSDGRGVKFF Size 1 ea Buffer In ascites fluid Preservative None Storage Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. GENE INFORMATION Gene Name VPS25 vacuolar protein sorting 25 homolog (S. cerevisiae) [ Homo sapiens ] 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Official Symbol VPS25 Synonyms VPS25; vacuolar protein sorting 25 homolog (S. cerevisiae);
[Show full text]
Endosome-Associated Complex, ESCRT-II, Recruits Transport Machinery for Protein Sorting at the Multivesicular Body
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Developmental Cell, Vol. 3, 283–289, August, 2002, Copyright 2002 by Cell Press Endosome-Associated Complex, ESCRT-II, Recruits Transport Machinery for Protein Sorting at the Multivesicular Body Markus Babst,2,4 David J. Katzmann,4 plays a critical role in the sorting of multiple cargo pro- William B. Snyder,2 Beverly Wendland,3 teins within the endosomal membrane system. and Scott D. Emr1 In a recent study, it has been demonstrated that sort- Department of Cellular and Molecular Medicine and ing of the yeast hydrolase carboxypeptidase S (CPS) Howard Hughes Medical Institute into the MVB pathway requires monoubiquitination of School of Medicine the short cytoplasmic tail of the protein (Katzmann et University of California, San Diego al., 2001). Mutations in CPS that block this ubiquitin La Jolla, California 92093 modification result in mislocalization of the protein to the limiting membrane of the vacuole. Furthermore, a protein complex called ESCRT-I (endosomal sorting complex required for transport) binds to ubiquitinated Summary CPS and thereby directs sorting of the hydrolase into the MVB pathway (Katzmann et al., 2001). ESCRT-I is Sorting of ubiquitinated endosomal membrane pro- composed of three different protein subunits (Vps23, teins into the MVB pathway is executed by the class Vps28, and Vps37) which belong to the class E vacuolar E Vps protein complexes ESCRT-I, -II, and -III, and protein sorting (Vps) proteins, a group of 15 proteins the AAA-type ATPase Vps4. This study characterizes required for proper endosomal function, including the ف ESCRT-II, a soluble 155 kDa protein complex formed formation of MVBs (Odorizzi et al., 1998).
[Show full text]
VPS25 Goat Polyclonal Antibody – TA303080 | Origene
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TA303080 VPS25 Goat Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: IHC, WB Recommended Dilution: ELISA: 1:1,000. WB: 0.5-1.5 µg/ml. IHC: 10µg/ml. Reactivity: Human (Expected from sequence similarity: Mouse, Rat, Dog) Host: Goat Isotype: IgG Clonality: Polyclonal Immunogen: Peptide with sequence C-QPNVDTRQKQ, from the internal region of the protein sequence according to NP_115729.1. Formulation: Supplied at 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. Concentration: lot specific Purification: Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide. Supplied at 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. Aliquot and store at -20°C. Minimize freezing and thawing. Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Gene Name: vacuolar protein sorting 25 homolog Database Link: NP_115729 Entrez Gene 28084 MouseEntrez Gene 681059 RatEntrez Gene 612774 DogEntrez Gene 84313 Human Q9BRG1 This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 VPS25 Goat Polyclonal Antibody – TA303080 Background: VPS25, VPS36 (MIM 610903), and SNF8 (MIM 610904) form ESCRT-II (endosomal sorting complex required for transport II), a complex involved in endocytosis of ubiquitinated membrane proteins.
[Show full text]
THE OLD and NEW FACE of CRANIOFACIAL RESEARCH: How Animal Models Inform Human Craniofacial Genetic and Clinical Data
HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author Dev Biol Manuscript Author . Author manuscript; Manuscript Author available in PMC 2017 July 15. Published in final edited form as: Dev Biol. 2016 July 15; 415(2): 171–187. doi:10.1016/j.ydbio.2016.01.017. THE OLD AND NEW FACE OF CRANIOFACIAL RESEARCH: How animal models inform human craniofacial genetic and clinical data Eric Van Otterloo, Trevor Williams, and Kristin B. Artinger Department of Craniofacial Biology, School of Dental Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA Kristin B. Artinger: [email protected] Abstract The craniofacial skeletal structures that comprise the human head develop from multiple tissues that converge to form the bones and cartilage of the face. Because of their complex development and morphogenesis, many human birth defects arise due to disruptions in these cellular populations. Thus, determining how these structures normally develop is vital if we are to gain a deeper understanding of craniofacial birth defects and devise treatment and prevention options. In this review, we will focus on how animal model systems have been used historically and in an ongoing context to enhance our understanding of human craniofacial development. We do this by first highlighting “animal to man” approaches: that is, how animal models are being utilized to understand fundamental mechanisms of craniofacial development. We discuss emerging technologies, including high throughput sequencing and genome editing, and new animal repository resources, and how their application can revolutionize the future of animal models in craniofacial research. Secondly, we highlight “man to animal” approaches, including the current use of animal models to test the function of candidate human disease variants.
[Show full text]
Downloaded from NCBI on December 361 5Th, 2020
bioRxiv preprint doi: https://doi.org/10.1101/2021.08.17.456605; this version posted August 17, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Characterisation of the Ubiquitin-ESCRT pathway in Asgard archaea sheds new light on 2 origins of membrane trafficking in eukaryotes 3 4 5 6 Tomoyuki Hatano1, Saravanan Palani1*, Dimitra Papatziamou2*, Diorge P. Souza3*, Ralf Salzer3*, 7 Daniel Tamarit4, 5* Mehul Makwana2, Antonia Potter2, Alexandra Haig2, Wenjue Xu2, David Townsend6, 8 David Rochester6, Dom Bellini3, Hamdi M. A. Hussain1, Thijs Ettema4, Jan Löwe3, Buzz Baum3§, 9 Nicholas P. Robinson2§, Mohan Balasubramanian1§ 10 11 12 13 1 Centre for Mechanochemical Cell Biology, Division of Biomedical Sciences, Warwick Medical School, 14 University of Warwick, Coventry CV4 7AL, United Kingdom 15 2 Division of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, 16 Lancaster LA1 4YG, United Kingdom 17 3 MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom 18 4 Laboratory of Microbiology, Department of Agrotechnology and Food Sciences, Wageningen 19 University, Wageningen 6708 WE, the Netherlands 20 5 Department of Aquatic Sciences and Assessment, Swedish University of Agricultural Sciences, SE- 21 75007 Uppsala, Sweden 22 6 Department of Chemistry, Lancaster University, Lancaster LA1 4YB, United Kingdom 23 24 25 *These authors contributed equally to this work and are listed alphabetically 26 27 28 29 § Correspondence to Mohan Balasubramanian- [email protected]; Nick 30 Robinson- [email protected] ; Buzz Baum- [email protected] 31 32 33 34 bioRxiv preprint doi: https://doi.org/10.1101/2021.08.17.456605; this version posted August 17, 2021.
[Show full text]
Agricultural University of Athens
ΓΕΩΠΟΝΙΚΟ ΠΑΝΕΠΙΣΤΗΜΙΟ ΑΘΗΝΩΝ ΣΧΟΛΗ ΕΠΙΣΤΗΜΩΝ ΤΩΝ ΖΩΩΝ ΤΜΗΜΑ ΕΠΙΣΤΗΜΗΣ ΖΩΙΚΗΣ ΠΑΡΑΓΩΓΗΣ ΕΡΓΑΣΤΗΡΙΟ ΓΕΝΙΚΗΣ ΚΑΙ ΕΙΔΙΚΗΣ ΖΩΟΤΕΧΝΙΑΣ ΔΙΔΑΚΤΟΡΙΚΗ ΔΙΑΤΡΙΒΗ Εντοπισμός γονιδιωματικών περιοχών και δικτύων γονιδίων που επηρεάζουν παραγωγικές και αναπαραγωγικές ιδιότητες σε πληθυσμούς κρεοπαραγωγικών ορνιθίων ΕΙΡΗΝΗ Κ. ΤΑΡΣΑΝΗ ΕΠΙΒΛΕΠΩΝ ΚΑΘΗΓΗΤΗΣ: ΑΝΤΩΝΙΟΣ ΚΟΜΙΝΑΚΗΣ ΑΘΗΝΑ 2020 ΔΙΔΑΚΤΟΡΙΚΗ ΔΙΑΤΡΙΒΗ Εντοπισμός γονιδιωματικών περιοχών και δικτύων γονιδίων που επηρεάζουν παραγωγικές και αναπαραγωγικές ιδιότητες σε πληθυσμούς κρεοπαραγωγικών ορνιθίων Genome-wide association analysis and gene network analysis for (re)production traits in commercial broilers ΕΙΡΗΝΗ Κ. ΤΑΡΣΑΝΗ ΕΠΙΒΛΕΠΩΝ ΚΑΘΗΓΗΤΗΣ: ΑΝΤΩΝΙΟΣ ΚΟΜΙΝΑΚΗΣ Τριμελής Επιτροπή: Aντώνιος Κομινάκης (Αν. Καθ. ΓΠΑ) Ανδρέας Κράνης (Eρευν. B, Παν. Εδιμβούργου) Αριάδνη Χάγερ (Επ. Καθ. ΓΠΑ) Επταμελής εξεταστική επιτροπή: Aντώνιος Κομινάκης (Αν. Καθ. ΓΠΑ) Ανδρέας Κράνης (Eρευν. B, Παν. Εδιμβούργου) Αριάδνη Χάγερ (Επ. Καθ. ΓΠΑ) Πηνελόπη Μπεμπέλη (Καθ. ΓΠΑ) Δημήτριος Βλαχάκης (Επ. Καθ. ΓΠΑ) Ευάγγελος Ζωίδης (Επ.Καθ. ΓΠΑ) Γεώργιος Θεοδώρου (Επ.Καθ. ΓΠΑ) 2 Εντοπισμός γονιδιωματικών περιοχών και δικτύων γονιδίων που επηρεάζουν παραγωγικές και αναπαραγωγικές ιδιότητες σε πληθυσμούς κρεοπαραγωγικών ορνιθίων Περίληψη Σκοπός της παρούσας διδακτορικής διατριβής ήταν ο εντοπισμός γενετικών δεικτών και υποψηφίων γονιδίων που εμπλέκονται στο γενετικό έλεγχο δύο τυπικών πολυγονιδιακών ιδιοτήτων σε κρεοπαραγωγικά ορνίθια. Μία ιδιότητα σχετίζεται με την ανάπτυξη (σωματικό βάρος στις 35 ημέρες, ΣΒ) και η άλλη με την αναπαραγωγική
[Show full text]
VPS25 (1-176, His-Tag) Human Protein – AR50272PU-N | Origene
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for AR50272PU-N VPS25 (1-176, His-tag) Human Protein Product data: Product Type: Recombinant Proteins Description: VPS25 (1-176, His-tag) human recombinant protein, 0.5 mg Species: Human Expression Host: E. coli Tag: His-tag Predicted MW: 23.3 kDa Concentration: lot specific Purity: >85% by SDS - PAGE Buffer: Presentation State: Purified State: Liquid purified protein Buffer System: 20 mM Tris-HCl buffer (pH8.0) containing 20% glycerol 0.1M Nacl Preparation: Liquid purified protein Protein Description: Recombinant human VPS25 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Storage: Store undiluted at 2-8°C for one week or (in aliquots) at -20°C to -80°C for longer. Avoid repeated freezing and thawing. Stability: Shelf life: one year from despatch. RefSeq: NP_115729 Locus ID: 84313 UniProt ID: Q9BRG1, A0A024R1X3 Cytogenetics: 17q21.2 Synonyms: DERP9; EAP20; FAP20 Summary: This gene encodes a protein that is a subunit of the endosomal sorting complex required for transport II (ESCRT-II). This protein complex functions in sorting of ubiquitinated membrane proteins during endocytosis. A pseudogene of this gene is present on chromosome 1. [provided by RefSeq, Jul 2013] Protein Families: Transcription Factors This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 VPS25 (1-176, His-tag) Human Protein – AR50272PU-N Protein Pathways: Endocytosis Product images: This product is to be used for laboratory only.
[Show full text]
ESCRT-III Activation by Parallel Action of ESCRT-I/II and ESCRT-0/Bro1
RESEARCH ADVANCE ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro1 during MVB biogenesis Shaogeng Tang1,2, Nicholas J Buchkovich1,2†, W Mike Henne1,2‡, Sudeep Banjade1,2, Yun Jung Kim1,2, Scott D Emr1,2* 1Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States; 2Department of Molecular Biology and Genetics, Cornell University, Ithaca, United States Abstract The endosomal sorting complexes required for transport (ESCRT) pathway facilitates multiple fundamental membrane remodeling events. Previously, we determined X-ray crystal structures of ESCRT-III subunit Snf7, the yeast CHMP4 ortholog, in its active and polymeric state (Tang et al., 2015). However, how ESCRT-III activation is coordinated by the upstream ESCRT components at endosomes remains unclear. Here, we provide a molecular explanation for the *For correspondence: sde26@ functional divergence of structurally similar ESCRT-III subunits. We characterize novel mutations in cornell.edu ESCRT-III Snf7 that trigger activation, and identify a novel role of Bro1, the yeast ALIX ortholog, in Snf7 assembly. We show that upstream ESCRTs regulate Snf7 activation at both its N-terminal core Present address: †Department domain and the C-terminus a6 helix through two parallel ubiquitin-dependent pathways: the of Microbiology and ESCRT-I-ESCRT-II-Vps20 pathway and the ESCRT-0-Bro1 pathway. We therefore provide an Immunology, The Pennsylvania State University College of enhanced understanding for the activation of the spatially unique ESCRT-III-mediated membrane Medicine, Hershey, United remodeling. States; ‡Department of Cell DOI: 10.7554/eLife.15507.001 Biology, The University of Texas Southwestern Medical Center, Dallas, United States Competing interests: The Introduction authors declare that no The endosomal sorting complex required for transport (ESCRT) pathway mediates topologically competing interests exist.
[Show full text]
Genome-Wide Rnai Screen Reveals a Role for the ESCRT Complex in Rotavirus Cell Entry
Genome-wide RNAi screen reveals a role for the ESCRT complex in rotavirus cell entry Daniela Silva-Ayalaa, Tomás Lópeza, Michelle Gutiérreza, Norbert Perrimonb, Susana Lópeza, and Carlos F. Ariasa,1 aDepartamento de Genética del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Colonia Chamilpa, Cuernavaca, Morelos 62210, Mexico; and bDepartment of Genetics, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115 Edited by Mary K. Estes, Baylor College of Medicine, Houston, TX, and approved May 3, 2013 (received for review March 14, 2013) Rotavirus (RV) is the major cause of childhood gastroenteritis described that the VP8 protein of human RV strain HAL1166 worldwide. This study presents a functional genome-scale analysis and the human RV strains belonging to the most frequent VP4 of cellular proteins and pathways relevant for RV infection using genotypes (P4 and P8) bind to A-type histo-blood group antigens RNAi. Among the 522 proteins selected in the screen for their (5, 6). Integrin 2β1 has also been reported to serve as an attach- ability to affect viral infectivity, an enriched group that partic- ment receptor for some RV strains (7), although this integrin, as ipates in endocytic processes was identiﬁed. Within these pro- well as integrins vβ3 and xβ2 and the heat-shock protein 70 teins, subunits of the vacuolar ATPase, small GTPases, actinin 4, (HSC70), have been implicated mostly in a postattachment in- and, of special interest, components of the endosomal sorting teraction of the virus that might be involved in cell internalization complex required for transport (ESCRT) machinery were found.
[Show full text]
The Vacuolar Protein Sorting Genes in Insects: a Comparative Genome View
Insect Biochemistry and Molecular Biology 62 (2015) 211e225 Contents lists available at ScienceDirect Insect Biochemistry and Molecular Biology journal homepage: www.elsevier.com/locate/ibmb The vacuolar protein sorting genes in insects: A comparative genome view * Zhaofei Li a, , Gary Blissard b a State Key Laboratory of Crop Stress Biology for Arid Areas, Key Laboratory of Northwest Loess Plateau Crop Pest Management of Ministry of Agriculture, College of Plant Protection, Northwest A&F University, Taicheng Road, Yangling, Shaanxi 712100, China b Boyce Thompson Institute, Cornell University, Ithaca, NY 14853, USA article info abstract Article history: In eukaryotic cells, regulated vesicular trafficking is critical for directing protein transport and for Received 3 September 2014 recycling and degradation of membrane lipids and proteins. Through carefully regulated transport Received in revised form vesicles, the endomembrane system performs a large and important array of dynamic cellular functions 6 November 2014 while maintaining the integrity of the cellular membrane system. Genetic studies in yeast Saccharomyces Accepted 21 November 2014 cerevisiae have identified approximately 50 vacuolar protein sorting (VPS) genes involved in vesicle Available online 5 December 2014 trafficking, and most of these genes are also characterized in mammals. The VPS proteins form distinct functional complexes, which include complexes known as ESCRT, retromer, CORVET, HOPS, GARP, and Keywords: VPS PI3K-III. Little is known about the orthologs of VPS proteins in insects. Here, with the newly annotated ESCRT Manduca sexta genome, we carried out genomic comparative analysis of VPS proteins in yeast, humans, Retromer and 13 sequenced insect genomes representing the Orders Hymenoptera, Diptera, Hemiptera, Phthir- VPS-C aptera, Lepidoptera, and Coleoptera.
[Show full text]