Signaling activations through G-protein-coupled-receptor aggregations

Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that observa...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:arXiv.org 2020-09
Hauptverfasser: Watabe, Masaki, Yoshimura, Hideaki, Arjunan, Satya N V, Kaizu, Kazunari, Takahashi, Koichi
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page
container_issue
container_start_page
container_title arXiv.org
container_volume
creator Watabe, Masaki
Yoshimura, Hideaki
Arjunan, Satya N V
Kaizu, Kazunari
Takahashi, Koichi
description Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that observable states of receptors can only take the form of monomers. Here, we propose a multiary complex model of GPCR signaling activations via the vector representation of various unobserved aggregated receptor states. Our results from model simulations imply that receptor aggregation processes can govern cooperative effects in a regime inaccessible by previous theories. In particular, we show how the affinity of ligand-receptor binding can be largely varied by various oligomer formations in the low concentration range of G-protein stimulus.
doi_str_mv 10.48550/arxiv.2004.07440
format Article
fullrecord <record><control><sourceid>proquest_arxiv</sourceid><recordid>TN_cdi_arxiv_primary_2004_07440</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2391022770</sourcerecordid><originalsourceid>FETCH-LOGICAL-a520-bd2c80486de8ddec113fd2ee380b2eed4d14c390b6ae840c3796a46f259e3bfc3</originalsourceid><addsrcrecordid>eNotj0FLwzAYhoMgOOZ-gCcLnlO_fEnb9ChjzsHAg7uXNPnaZdS2pu3Qf2_dPD2Xh5f3YexBQKx0ksCzCd_-HCOAiiFTCm7YAqUUXCvEO7YahhMAYJphksgF23z4ujWNb-vI2NGfzei7dojGY-im-hhteR-6kXzLbTf1DTkeyFI_diEydR2ovvr37LYyzUCrfy7Z4XVzWL_x_ft2t37Zc5Mg8NKh1aB06kg7R1YIWTkkkhrKGU45oazMoUwNaQVWZnlqVFphkpMsKyuX7PE6e2ks-uA_Tfgp_lqLS-tsPF2N-fbXRMNYnLopzIFDgTIXgJhlIH8BEdRYVg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2391022770</pqid></control><display><type>article</type><title>Signaling activations through G-protein-coupled-receptor aggregations</title><source>arXiv.org</source><source>Free E- Journals</source><creator>Watabe, Masaki ; Yoshimura, Hideaki ; Arjunan, Satya N V ; Kaizu, Kazunari ; Takahashi, Koichi</creator><creatorcontrib>Watabe, Masaki ; Yoshimura, Hideaki ; Arjunan, Satya N V ; Kaizu, Kazunari ; Takahashi, Koichi</creatorcontrib><description>Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that observable states of receptors can only take the form of monomers. Here, we propose a multiary complex model of GPCR signaling activations via the vector representation of various unobserved aggregated receptor states. Our results from model simulations imply that receptor aggregation processes can govern cooperative effects in a regime inaccessible by previous theories. In particular, we show how the affinity of ligand-receptor binding can be largely varied by various oligomer formations in the low concentration range of G-protein stimulus.</description><identifier>EISSN: 2331-8422</identifier><identifier>DOI: 10.48550/arxiv.2004.07440</identifier><language>eng</language><publisher>Ithaca: Cornell University Library, arXiv.org</publisher><subject>Agglomeration ; Complex formation ; Computer simulation ; Formations ; Ligands ; Proteins ; Quantitative Biology - Biomolecules ; Quantitative Biology - Molecular Networks ; Receptors ; Signaling</subject><ispartof>arXiv.org, 2020-09</ispartof><rights>2020. This work is published under http://arxiv.org/licenses/nonexclusive-distrib/1.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>http://arxiv.org/licenses/nonexclusive-distrib/1.0</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>228,230,777,781,882,27906</link.rule.ids><backlink>$$Uhttps://doi.org/10.48550/arXiv.2004.07440$$DView paper in arXiv$$Hfree_for_read</backlink><backlink>$$Uhttps://doi.org/10.1103/PhysRevE.102.032413$$DView published paper (Access to full text may be restricted)$$Hfree_for_read</backlink></links><search><creatorcontrib>Watabe, Masaki</creatorcontrib><creatorcontrib>Yoshimura, Hideaki</creatorcontrib><creatorcontrib>Arjunan, Satya N V</creatorcontrib><creatorcontrib>Kaizu, Kazunari</creatorcontrib><creatorcontrib>Takahashi, Koichi</creatorcontrib><title>Signaling activations through G-protein-coupled-receptor aggregations</title><title>arXiv.org</title><description>Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that observable states of receptors can only take the form of monomers. Here, we propose a multiary complex model of GPCR signaling activations via the vector representation of various unobserved aggregated receptor states. Our results from model simulations imply that receptor aggregation processes can govern cooperative effects in a regime inaccessible by previous theories. In particular, we show how the affinity of ligand-receptor binding can be largely varied by various oligomer formations in the low concentration range of G-protein stimulus.</description><subject>Agglomeration</subject><subject>Complex formation</subject><subject>Computer simulation</subject><subject>Formations</subject><subject>Ligands</subject><subject>Proteins</subject><subject>Quantitative Biology - Biomolecules</subject><subject>Quantitative Biology - Molecular Networks</subject><subject>Receptors</subject><subject>Signaling</subject><issn>2331-8422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GOX</sourceid><recordid>eNotj0FLwzAYhoMgOOZ-gCcLnlO_fEnb9ChjzsHAg7uXNPnaZdS2pu3Qf2_dPD2Xh5f3YexBQKx0ksCzCd_-HCOAiiFTCm7YAqUUXCvEO7YahhMAYJphksgF23z4ujWNb-vI2NGfzei7dojGY-im-hhteR-6kXzLbTf1DTkeyFI_diEydR2ovvr37LYyzUCrfy7Z4XVzWL_x_ft2t37Zc5Mg8NKh1aB06kg7R1YIWTkkkhrKGU45oazMoUwNaQVWZnlqVFphkpMsKyuX7PE6e2ks-uA_Tfgp_lqLS-tsPF2N-fbXRMNYnLopzIFDgTIXgJhlIH8BEdRYVg</recordid><startdate>20200922</startdate><enddate>20200922</enddate><creator>Watabe, Masaki</creator><creator>Yoshimura, Hideaki</creator><creator>Arjunan, Satya N V</creator><creator>Kaizu, Kazunari</creator><creator>Takahashi, Koichi</creator><general>Cornell University Library, arXiv.org</general><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>L6V</scope><scope>M7S</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>ALC</scope><scope>GOX</scope></search><sort><creationdate>20200922</creationdate><title>Signaling activations through G-protein-coupled-receptor aggregations</title><author>Watabe, Masaki ; Yoshimura, Hideaki ; Arjunan, Satya N V ; Kaizu, Kazunari ; Takahashi, Koichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a520-bd2c80486de8ddec113fd2ee380b2eed4d14c390b6ae840c3796a46f259e3bfc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Agglomeration</topic><topic>Complex formation</topic><topic>Computer simulation</topic><topic>Formations</topic><topic>Ligands</topic><topic>Proteins</topic><topic>Quantitative Biology - Biomolecules</topic><topic>Quantitative Biology - Molecular Networks</topic><topic>Receptors</topic><topic>Signaling</topic><toplevel>online_resources</toplevel><creatorcontrib>Watabe, Masaki</creatorcontrib><creatorcontrib>Yoshimura, Hideaki</creatorcontrib><creatorcontrib>Arjunan, Satya N V</creatorcontrib><creatorcontrib>Kaizu, Kazunari</creatorcontrib><creatorcontrib>Takahashi, Koichi</creatorcontrib><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Engineering Collection</collection><collection>Engineering Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>arXiv Quantitative Biology</collection><collection>arXiv.org</collection><jtitle>arXiv.org</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watabe, Masaki</au><au>Yoshimura, Hideaki</au><au>Arjunan, Satya N V</au><au>Kaizu, Kazunari</au><au>Takahashi, Koichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Signaling activations through G-protein-coupled-receptor aggregations</atitle><jtitle>arXiv.org</jtitle><date>2020-09-22</date><risdate>2020</risdate><eissn>2331-8422</eissn><abstract>Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that observable states of receptors can only take the form of monomers. Here, we propose a multiary complex model of GPCR signaling activations via the vector representation of various unobserved aggregated receptor states. Our results from model simulations imply that receptor aggregation processes can govern cooperative effects in a regime inaccessible by previous theories. In particular, we show how the affinity of ligand-receptor binding can be largely varied by various oligomer formations in the low concentration range of G-protein stimulus.</abstract><cop>Ithaca</cop><pub>Cornell University Library, arXiv.org</pub><doi>10.48550/arxiv.2004.07440</doi><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier EISSN: 2331-8422
ispartof arXiv.org, 2020-09
issn 2331-8422
language eng
recordid cdi_arxiv_primary_2004_07440
source arXiv.org; Free E- Journals
subjects Agglomeration
Complex formation
Computer simulation
Formations
Ligands
Proteins
Quantitative Biology - Biomolecules
Quantitative Biology - Molecular Networks
Receptors
Signaling
title Signaling activations through G-protein-coupled-receptor aggregations
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T13%3A57%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_arxiv&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Signaling%20activations%20through%20G-protein-coupled-receptor%20aggregations&rft.jtitle=arXiv.org&rft.au=Watabe,%20Masaki&rft.date=2020-09-22&rft.eissn=2331-8422&rft_id=info:doi/10.48550/arxiv.2004.07440&rft_dat=%3Cproquest_arxiv%3E2391022770%3C/proquest_arxiv%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2391022770&rft_id=info:pmid/&rfr_iscdi=true