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  1. AU="Nakos, Konstantinos"
  2. AU="Schreiner, Ryan"
  3. AU=Pltz T
  4. AU="Akhmanova, Anna" AU="Akhmanova, Anna"
  5. AU="Goretsky, Anton"
  6. AU="Cordoza, Makayla L"
  7. AU=Midoux Patrick AU=Midoux Patrick
  8. AU="Mundt, H M"
  9. AU=Tsivitse Susan

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  1. Artikel ; Online: Cellular functions of actin- and microtubule-associated septins.

    Spiliotis, Elias T / Nakos, Konstantinos

    Current biology : CB

    2021  Band 31, Heft 10, Seite(n) R651–R666

    Abstract: Septins are an integral component of the cytoskeleton, assembling into higher-order oligomers and filamentous polymers that associate with actin filaments, microtubules and membranes. Here, we review septin interactions with actin and microtubules, and ... ...

    Abstract Septins are an integral component of the cytoskeleton, assembling into higher-order oligomers and filamentous polymers that associate with actin filaments, microtubules and membranes. Here, we review septin interactions with actin and microtubules, and septin-mediated regulation of the organization and dynamics of these cytoskeletal networks, which is critical for cellular morphogenesis. We discuss how actomyosin-associated septins function in cytokinesis, cell migration and host defense against pathogens. We highlight newly emerged roles of septins at the interface of microtubules and membranes with molecular motors, which point to a 'septin code' for the regulation of membrane traffic. Additionally, we revisit the functions of microtubule-associated septins in mitosis and meiosis. In sum, septins comprise a unique module of cytoskeletal regulators that are spatially and functionally specialized and have properties of bona fide actin-binding and microtubule-associated proteins. With many questions still outstanding, the study of septins will continue to provide new insights into fundamental problems of cytoskeletal organization and function.
    Mesh-Begriff(e) Actin Cytoskeleton/metabolism ; Actins/metabolism ; Animals ; Humans ; Microtubules/metabolism ; Septins/metabolism
    Chemische Substanzen Actins ; Septins (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2021-05-24
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2021.03.064
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Microtubule-associated septin complexes modulate kinesin and dynein motility with differential specificities.

    Suber, Yani / Alam, Md Noor A / Nakos, Konstantinos / Bhakt, Priyanka / Spiliotis, Elias T

    The Journal of biological chemistry

    2023  Band 299, Heft 9, Seite(n) 105084

    Abstract: Long-range membrane traffic is guided by microtubule-associated proteins and posttranslational modifications, which collectively comprise a traffic code. The regulatory principles of this code and how it orchestrates the motility of kinesin and dynein ... ...

    Abstract Long-range membrane traffic is guided by microtubule-associated proteins and posttranslational modifications, which collectively comprise a traffic code. The regulatory principles of this code and how it orchestrates the motility of kinesin and dynein motors are largely unknown. Septins are a large family of GTP-binding proteins, which assemble into complexes that associate with microtubules. Using single-molecule in vitro motility assays, we tested how the microtubule-associated SEPT2/6/7, SEPT2/6/7/9, and SEPT5/7/11 complexes affect the motilities of the constitutively active kinesins KIF5C and KIF1A and the dynein-dynactin-bicaudal D (DDB) motor complex. We found that microtubule-associated SEPT2/6/7 is a potent inhibitor of DDB and KIF5C, preventing mainly their association with microtubules. SEPT2/6/7 also inhibits KIF1A by obstructing stepping along microtubules. On SEPT2/6/7/9-coated microtubules, KIF1A inhibition is dampened by SEPT9, which alone enhances KIF1A, showing that individual septin subunits determine the regulatory properties of septin complexes. Strikingly, SEPT5/7/11 differs from SEPT2/6/7, in permitting the motility of KIF1A and immobilizing DDB to the microtubule lattice. In hippocampal neurons, filamentous SEPT5 colocalizes with somatodendritic microtubules that underlie Golgi membranes and lack SEPT6. Depletion of SEPT5 disrupts Golgi morphology and polarization of Golgi ribbons into the shaft of somato-proximal dendrites, which is consistent with the tethering of DDB to microtubules by SEPT5/7/11. Collectively, these results suggest that microtubule-associated complexes have differential specificities in the regulation of the motility and positioning of microtubule motors. We posit that septins are an integral part of the microtubule-based code that spatially controls membrane traffic.
    Mesh-Begriff(e) Dyneins/metabolism ; Kinesins/metabolism ; Microtubule-Associated Proteins/metabolism ; Septins/metabolism ; COS Cells ; HEK293 Cells ; Humans ; Animals ; Chlorocebus aethiops ; Protein Transport
    Chemische Substanzen DDB (8065-92-7) ; Dyneins (EC 3.6.4.2) ; Kinesins (EC 3.6.4.4) ; Microtubule-Associated Proteins ; Septins (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2023-07-24
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.105084
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Septin 2/6/7 complexes tune microtubule plus-end growth and EB1 binding in a concentration- and filament-dependent manner.

    Nakos, Konstantinos / Radler, Megan R / Spiliotis, Elias T

    Molecular biology of the cell

    2019  Band 30, Heft 23, Seite(n) 2913–2928

    Abstract: Septins (SEPTs) are filamentous guanosine-5'-triphosphate (GTP)-binding proteins, which affect microtubule (MT)-dependent functions including membrane trafficking and cell division, but their precise role in MT dynamics is poorly understood. Here, in ... ...

    Abstract Septins (SEPTs) are filamentous guanosine-5'-triphosphate (GTP)-binding proteins, which affect microtubule (MT)-dependent functions including membrane trafficking and cell division, but their precise role in MT dynamics is poorly understood. Here, in vitro reconstitution of MT dynamics with SEPT2/6/7, the minimal subunits of septin heteromers, shows that SEPT2/6/7 has a biphasic concentration-dependent effect on MT growth. Lower concentrations of SEPT2/6/7 enhance MT plus-end growth and elongation, while higher and intermediate concentrations inhibit and pause plus-end growth, respectively. We show that SEPT2/6/7 has a modest preference for GTP- over guanosine diphosphate (GDP)-bound MT lattice and competes with end-binding protein 1 (EB1) for binding to guanosine 5'-
    Mesh-Begriff(e) Animals ; Humans ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Models, Biological ; Multiprotein Complexes/metabolism ; Protein Binding ; Rats, Sprague-Dawley ; Septins/metabolism
    Chemische Substanzen EB1 microtubule binding proteins ; Microtubule-Associated Proteins ; Multiprotein Complexes ; Septins (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2019-10-02
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E19-07-0362
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Regulation of microtubule plus end dynamics by septin 9.

    Nakos, Konstantinos / Rosenberg, Marshall / Spiliotis, Elias T

    Cytoskeleton (Hoboken, N.J.)

    2018  Band 76, Heft 1, Seite(n) 83–91

    Abstract: Septins are GTP-binding proteins that associate with the microtubule (MT) and actin cytoskeleton. Septins affect MT organization and posttranslational modifications, but their role in MT dynamics is less understood. Here, we reconstituted MT dynamics in ... ...

    Abstract Septins are GTP-binding proteins that associate with the microtubule (MT) and actin cytoskeleton. Septins affect MT organization and posttranslational modifications, but their role in MT dynamics is less understood. Here, we reconstituted MT dynamics in the presence of the MT-binding septin (SEPT9) using an in vitro cell-free assay, which images the polymerization of tubulin from guanosine-5'-[(α,β)-methyleno]triphosphate (GMPCPP)-stabilized MT seeds. We found that submicromolar concentrations of SEPT9 suppress MT catastrophe and enhance the growth of MT plus ends to great lengths, while low micromolar concentrations of SEPT9 stabilize MTs by inhibiting dynamic instability. We show that SEPT9 associates preferentially with the lattice of GMPCPP-stabilized MT seeds and surprisingly recruits soluble tubulin to the MT lattice. Notably, the effects of SEPT9 on MT dynamics are dependent on its G-G dimerization interface, which is formed by the pockets of the GTP-binding domains. A mutation (H530D) that disrupts G-G dimerization abrogates the effects of SEPT9 on MT dynamics and diminishes its ability to recruit tubulin to the MT lattice. Taken together, these results suggest that SEPT9 promotes the formation and maintenance of long stable MTs through a mechanism that may involve recruitment of unpolymerized tubulin to the MT lattice.
    Mesh-Begriff(e) Microscopy ; Microtubules/metabolism ; Septins/metabolism ; Tubulin/metabolism
    Chemische Substanzen Tubulin ; Septins (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2018-11-14
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2534372-5
    ISSN 1949-3592 ; 1949-3584
    ISSN (online) 1949-3592
    ISSN 1949-3584
    DOI 10.1002/cm.21488
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Septins guide noncentrosomal microtubules to promote focal adhesion disassembly in migrating cells.

    Merenich, Daniel / Nakos, Konstantinos / Pompan, Taylor / Donovan, Samantha J / Gill, Amrik / Patel, Pranav / Spiliotis, Elias T / Myers, Kenneth A

    Molecular biology of the cell

    2022  Band 33, Heft 5, Seite(n) ar40

    Abstract: Endothelial cell migration is critical for vascular angiogenesis and is compromised to facilitate tumor metastasis. The migratory process requires the coordinated assembly and disassembly of focal adhesions (FA), actin, and microtubules (MT). MT dynamics ...

    Abstract Endothelial cell migration is critical for vascular angiogenesis and is compromised to facilitate tumor metastasis. The migratory process requires the coordinated assembly and disassembly of focal adhesions (FA), actin, and microtubules (MT). MT dynamics at FAs deliver vesicular cargoes and enhance actomyosin contractility to promote FA turnover and facilitate cell advance. Noncentrosomal (NC) MTs regulate FA dynamics and are sufficient to drive cell polarity, but how NC MTs target FAs to control FA turnover is not understood. Here, we show that Rac1 induces the assembly of FA-proximal septin filaments that promote NC MT growth into FAs and inhibit mitotic centromere-associated kinesin (MCAK)-associated MT disassembly, thereby maintaining intact MT plus ends proximal to FAs. Septin-associated MT rescue is coupled with accumulation of Aurora-A kinase and cytoplasmic linker-associated protein (CLASP) localization to the MT between septin and FAs. In this way, NC MTs are strategically positioned to undergo MCAK- and CLASP-regulated bouts of assembly and disassembly into FAs, thereby regulating FA turnover and cell migration.
    Mesh-Begriff(e) Actin Cytoskeleton/metabolism ; Actins/metabolism ; Cell Movement/physiology ; Focal Adhesions/metabolism ; Microtubules/metabolism ; Septins/metabolism
    Chemische Substanzen Actins ; Septins (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2022-03-11
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E21-06-0334
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel: Torques within and outside the human spindle balance twist at anaphase.

    Neahring, Lila / He, Yifei / Cho, Nathan H / Liu, Gaoxiang / Fernandes, Jonathan / Rux, Caleb J / Nakos, Konstantinos / Subramanian, Radhika / Upadhyayula, Srigokul / Yildiz, Ahmet / Dumont, Sophie

    bioRxiv : the preprint server for biology

    2023  

    Abstract: At each cell division, nanometer-scale motors and microtubules give rise to the micron-scale spindle. Many mitotic motors step helically around microtubules in vitro, and most are predicted to twist the spindle in a left-handed direction. However, the ... ...

    Abstract At each cell division, nanometer-scale motors and microtubules give rise to the micron-scale spindle. Many mitotic motors step helically around microtubules in vitro, and most are predicted to twist the spindle in a left-handed direction. However, the human spindle exhibits only slight global twist, raising the question of how these molecular torques are balanced. Here, using lattice light sheet microscopy, we find that anaphase spindles in the epithelial cell line MCF10A have a high baseline twist, and we identify factors that both increase and decrease this twist. The midzone motors KIF4A and MKLP1 are redundantly required for left-handed twist at anaphase, and we show that KIF4A generates left-handed torque in vitro. The actin cytoskeleton also contributes to left-handed twist, but dynein and its cortical recruitment factor LGN counteract it. Together, our work demonstrates that force generators regulate twist in opposite directions from both within and outside the spindle, preventing strong spindle twist during chromosome segregation.
    Sprache Englisch
    Erscheinungsdatum 2023-12-10
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.12.10.570990
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells.

    Devlin, Louis / Okletey, Joshua / Perkins, George / Bowen, Jonathan R / Nakos, Konstantinos / Montagna, Cristina / Spiliotis, Elias T

    Proteomics

    2021  Band 21, Heft 19, Seite(n) e2100155

    Abstract: Septins are a family of multimeric GTP-binding proteins, which are abnormally expressed in cancer. Septin 9 (SEPT9) is an essential and ubiquitously expressed septin with multiple isoforms, which have differential expression patterns and effects in ... ...

    Abstract Septins are a family of multimeric GTP-binding proteins, which are abnormally expressed in cancer. Septin 9 (SEPT9) is an essential and ubiquitously expressed septin with multiple isoforms, which have differential expression patterns and effects in breast cancer cells. It is unknown, however, if SEPT9 isoforms associate with different molecular networks and functions. Here, we performed a proteomic screen in MCF-7 breast cancer cells to identify the interactome of GFP-SEPT9 isoforms 1, 4 and 5, which vary significantly in their N-terminal extensions. While all three isoforms associated with SEPT2 and SEPT7, the truncated SEPT9_i4 and SEPT9_i5 interacted with septins of the SEPT6 group more promiscuously than SEPT9_i1, which bound predominately SEPT8. Spatial mapping and functional clustering of non-septin partners showed isoform-specific differences in interactions with proteins of distinct subcellular organelles (e.g., nuclei, centrosomes, cilia) and functions such as cell signalling and ubiquitination. The interactome of the full length SEPT9_i1 was more enriched in cytoskeletal regulators, while the truncated SEPT9_i4 and SEPT9_i5 exhibited preferential and isoform-specific interactions with nuclear, signalling, and ubiquitinating proteins. These data provide evidence for isoform-specific interactions, which arise from truncations in the N-terminal extensions of SEPT9, and point to novel roles in the pathogenesis of breast cancer.
    Mesh-Begriff(e) Breast Neoplasms ; Female ; Gene Expression Profiling ; Humans ; MCF-7 Cells ; Protein Isoforms/genetics ; Proteomics ; Septins/genetics ; Septins/metabolism
    Chemische Substanzen Protein Isoforms ; SEPTIN9 protein, human (EC 3.6.1.-) ; Septins (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2021-08-31
    Erscheinungsland Germany
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2032093-0
    ISSN 1615-9861 ; 1615-9853
    ISSN (online) 1615-9861
    ISSN 1615-9853
    DOI 10.1002/pmic.202100155
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel: Measuring workflow knowledge-base effectiveness for an in-house banking customer service call center

    Karakerezis, Angelos / Nakos, Konstantinos

    Computational techniques for banking and risk management , p. 115-126

    2013  , Seite(n) 115–126

    Verfasserangabe Angelos Karakerezis and Konstantinos Nakos
    Schlagwörter Informationstechnik ; Unternehmensorganisation ; Bankgeschäft ; Kundenservice ; Callcenter ; Griechenland
    Sprache Englisch
    Umfang graph. Darst.
    Verlag Nova Publ.
    Erscheinungsort New York, NY
    Dokumenttyp Artikel
    ISBN 978-1-62618-522-7 ; 1-62618-522-0
    Datenquelle ECONomics Information System

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  9. Artikel ; Online: A Septin Double Ring Controls the Spatiotemporal Organization of the ESCRT Machinery in Cytokinetic Abscission.

    Karasmanis, Eva P / Hwang, Daniel / Nakos, Konstantinos / Bowen, Jonathan R / Angelis, Dimitrios / Spiliotis, Elias T

    Current biology : CB

    2019  Band 29, Heft 13, Seite(n) 2174–2182.e7

    Abstract: Abscission is the terminal step of mitosis that physically separates two daughter cells [1, 2]. Abscission requires the endocytic sorting complex required for transport (ESCRT), a molecular machinery of multiple subcomplexes (ESCRT-I/II/III) that ... ...

    Abstract Abscission is the terminal step of mitosis that physically separates two daughter cells [1, 2]. Abscission requires the endocytic sorting complex required for transport (ESCRT), a molecular machinery of multiple subcomplexes (ESCRT-I/II/III) that promotes membrane remodeling and scission [3-5]. Recruitment of ESCRT-I/II complexes to the midbody of telophase cells initiates ESCRT-III assembly into two rings, which subsequently expand into helices and spirals that narrow down to the incipient site of abscission [6-8]. ESCRT-III assembly is highly dynamic and spatiotemporally ordered, but the underlying mechanisms are poorly understood. Here, we report that, after cleavage furrow closure, septins form a membrane-bound double ring that controls the organization and function of ESCRT-III. The septin double ring demarcates the sites of ESCRT-III assembly into rings and disassembles before ESCRT-III rings expand into helices and spirals. We show that septin 9 (SEPT9) depletion, which abrogates abscission, impairs recruitment of VPS25 (ESCRT-II) and CHMP6 (ESCRT-III). Strikingly, ESCRT-III subunits (CHMP4B and CHMP2A/B) accumulate to the midbody, but they are highly disorganized, failing to form symmetric rings and to expand laterally into the cone-shaped helices and spirals of abscission. We found that SEPT9 interacts directly with the ubiquitin E2 variant (UEV) domain of ESCRT-I protein TSG101 through two N-terminal PTAP motifs, which are required for the recruitment of VPS25 and CHMP6, and the spatial organization of ESCRT-III (CHMP4B and CHMP2B) into functional rings. These results reveal that septins function in the ESCRT-I-ESCRT-II-CHMP6 pathway of ESCRT-III assembly and provide a framework for the spatiotemporal control of the ESCRT machinery of cytokinetic abscission.
    Mesh-Begriff(e) Animals ; Cytokinesis ; Cytoskeleton/metabolism ; Dogs ; Endosomal Sorting Complexes Required for Transport/metabolism ; Madin Darby Canine Kidney Cells ; Mitosis ; Septins/metabolism
    Chemische Substanzen Endosomal Sorting Complexes Required for Transport ; Septins (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2019-06-13
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2019.05.050
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Septins mediate a microtubule-actin crosstalk that enables actin growth on microtubules.

    Nakos, Konstantinos / Alam, Md Noor A / Radler, Megan R / Kesisova, Ilona A / Yang, Changsong / Okletey, Joshua / Tomasso, Meagan R / Padrick, Shae B / Svitkina, Tatyana M / Spiliotis, Elias T

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Band 119, Heft 50, Seite(n) e2202803119

    Abstract: Cellular morphogenesis and processes such as cell division and migration require the coordination of the microtubule and actin cytoskeletons. Microtubule-actin crosstalk is poorly understood and largely regarded as the capture and regulation of ... ...

    Abstract Cellular morphogenesis and processes such as cell division and migration require the coordination of the microtubule and actin cytoskeletons. Microtubule-actin crosstalk is poorly understood and largely regarded as the capture and regulation of microtubules by actin. Septins are filamentous guanosine-5'-triphosphate (GTP) binding proteins, which comprise the fourth component of the cytoskeleton along microtubules, actin, and intermediate filaments. Here, we report that septins mediate microtubule-actin crosstalk by coupling actin polymerization to microtubule lattices. Superresolution and platinum replica electron microscopy (PREM) show that septins localize to overlapping microtubules and actin filaments in the growth cones of neurons and non-neuronal cells. We demonstrate that recombinant septin complexes directly crosslink microtubules and actin filaments into hybrid bundles. In vitro reconstitution assays reveal that microtubule-bound septins capture and align stable actin filaments with microtubules. Strikingly, septins enable the capture and polymerization of growing actin filaments on microtubule lattices. In neuronal growth cones, septins are required for the maintenance of the peripheral actin network that fans out from microtubules. These findings show that septins directly mediate microtubule interactions with actin filaments, and reveal a mechanism of microtubule-templated actin growth with broader significance for the self-organization of the cytoskeleton and cellular morphogenesis.
    Mesh-Begriff(e) Septins ; Actins ; Microtubules
    Chemische Substanzen Septins (EC 3.6.1.-) ; Actins
    Sprache Englisch
    Erscheinungsdatum 2022-12-07
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2202803119
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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