Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells

Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. Three homologous genes, CNN1, CNN2 and CNN3, encoding calponin isoforms 1, 2, and 3, respectively, are present in vertebrate species. All three calponin isoforms are actin-bindi...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Gene 2016-07, Vol.585 (1), p.143-153
Hauptverfasser: Liu, Rong, Jin, J.-P.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 153
container_issue 1
container_start_page 143
container_title Gene
container_volume 585
creator Liu, Rong
Jin, J.-P.
description Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. Three homologous genes, CNN1, CNN2 and CNN3, encoding calponin isoforms 1, 2, and 3, respectively, are present in vertebrate species. All three calponin isoforms are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton, while each isoform executes different physiological roles based on their cell type-specific expressions. Calponin 1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin 2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin 3 participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Phosphorylation has been extensively studied for the regulation of calponin functions. Cytoskeleton tension regulates the transcription of CNN2 gene and the degradation of calponin 2 protein. This review summarizes our knowledge learned from studies over the past three decades, focusing on the evolutionary lineage of calponin isoform genes, their tissue- and cell type-specific expressions, structure–function relationships, and mechanoregulation.
doi_str_mv 10.1016/j.gene.2016.02.040
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5325697</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0378111916301238</els_id><sourcerecordid>1825425378</sourcerecordid><originalsourceid>FETCH-LOGICAL-e385t-fcc26f6925e841ae985dd382ce8f022d43bfd5d01dcf180f55dbec28519a3aad3</originalsourceid><addsrcrecordid>eNqNUk1v1DAQtSoQXVr-QA_IRw4k-CNOnAohoRVfUlWkCs6W1x5vvST2EjsV_fc4dFvRE_hgjz1vnjxvHkJnlNSU0PbNrt5CgJqVuCasJg05Qisqu74ihMsnaEV4JytKaX-Mnqe0I2UJwZ6hY9b2HaFdu0K_1nrYx-AD9im6OI0Jry8v6etlZ1gHuwT8HF_Bdh50jlPCBYW1yaXE3OaYfsAAOQbs5lAeY0i4ZNIYY77G45zMAH9oQgzV4WpgGNIpeur0kODF4TxB3z9--Lb-XF18_fRl_f6iAi5FrpwxrHVtzwTIhmropbCWS2ZAOsKYbfjGWWEJtcZRSZwQdgOGSUF7zbW2_AS9u-Pdz5sRrIGQJz2o_eRHPd2qqL16nAn-Wm3jjRKciSJTIXh1IJjizxlSVqNPSws6QJyTopKJhoki9b-hXRlO13YN_R8o57wXhBXoy787ePj6_RAL4O0dAIqONx4mlYyHYMD6CUxWNnpFiVo8o3Zq8YxaPKMIU8Uz_DfMerVZ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1783339502</pqid></control><display><type>article</type><title>Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Liu, Rong ; Jin, J.-P.</creator><creatorcontrib>Liu, Rong ; Jin, J.-P.</creatorcontrib><description>Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. Three homologous genes, CNN1, CNN2 and CNN3, encoding calponin isoforms 1, 2, and 3, respectively, are present in vertebrate species. All three calponin isoforms are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton, while each isoform executes different physiological roles based on their cell type-specific expressions. Calponin 1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin 2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin 3 participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Phosphorylation has been extensively studied for the regulation of calponin functions. Cytoskeleton tension regulates the transcription of CNN2 gene and the degradation of calponin 2 protein. This review summarizes our knowledge learned from studies over the past three decades, focusing on the evolutionary lineage of calponin isoform genes, their tissue- and cell type-specific expressions, structure–function relationships, and mechanoregulation.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/j.gene.2016.02.040</identifier><identifier>PMID: 26970176</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>actin ; Actin cytoskeleton ; Actin Cytoskeleton - metabolism ; Calcium-Binding Proteins - genetics ; Calponin isoform genes ; Calponins ; Cell Movement ; embryogenesis ; genes ; Humans ; Mechanoreceptors - metabolism ; Mechanoregulation ; Microfilament Proteins - genetics ; microfilaments ; Muscle Contraction - physiology ; muscle development ; muscle strength ; myocytes ; Myocytes, Smooth Muscle - metabolism ; myosin ; Myosins - metabolism ; Non-muscle cell motility ; Organ Specificity - genetics ; phosphorylation ; Protein Isoforms - genetics ; regulatory proteins ; Smooth muscle ; Structure-Activity Relationship ; structure-activity relationships ; vertebrates</subject><ispartof>Gene, 2016-07, Vol.585 (1), p.143-153</ispartof><rights>2016 Elsevier B.V.</rights><rights>Copyright © 2016 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0378111916301238$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26970176$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Rong</creatorcontrib><creatorcontrib>Jin, J.-P.</creatorcontrib><title>Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells</title><title>Gene</title><addtitle>Gene</addtitle><description>Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. Three homologous genes, CNN1, CNN2 and CNN3, encoding calponin isoforms 1, 2, and 3, respectively, are present in vertebrate species. All three calponin isoforms are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton, while each isoform executes different physiological roles based on their cell type-specific expressions. Calponin 1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin 2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin 3 participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Phosphorylation has been extensively studied for the regulation of calponin functions. Cytoskeleton tension regulates the transcription of CNN2 gene and the degradation of calponin 2 protein. This review summarizes our knowledge learned from studies over the past three decades, focusing on the evolutionary lineage of calponin isoform genes, their tissue- and cell type-specific expressions, structure–function relationships, and mechanoregulation.</description><subject>actin</subject><subject>Actin cytoskeleton</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calponin isoform genes</subject><subject>Calponins</subject><subject>Cell Movement</subject><subject>embryogenesis</subject><subject>genes</subject><subject>Humans</subject><subject>Mechanoreceptors - metabolism</subject><subject>Mechanoregulation</subject><subject>Microfilament Proteins - genetics</subject><subject>microfilaments</subject><subject>Muscle Contraction - physiology</subject><subject>muscle development</subject><subject>muscle strength</subject><subject>myocytes</subject><subject>Myocytes, Smooth Muscle - metabolism</subject><subject>myosin</subject><subject>Myosins - metabolism</subject><subject>Non-muscle cell motility</subject><subject>Organ Specificity - genetics</subject><subject>phosphorylation</subject><subject>Protein Isoforms - genetics</subject><subject>regulatory proteins</subject><subject>Smooth muscle</subject><subject>Structure-Activity Relationship</subject><subject>structure-activity relationships</subject><subject>vertebrates</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUk1v1DAQtSoQXVr-QA_IRw4k-CNOnAohoRVfUlWkCs6W1x5vvST2EjsV_fc4dFvRE_hgjz1vnjxvHkJnlNSU0PbNrt5CgJqVuCasJg05Qisqu74ihMsnaEV4JytKaX-Mnqe0I2UJwZ6hY9b2HaFdu0K_1nrYx-AD9im6OI0Jry8v6etlZ1gHuwT8HF_Bdh50jlPCBYW1yaXE3OaYfsAAOQbs5lAeY0i4ZNIYY77G45zMAH9oQgzV4WpgGNIpeur0kODF4TxB3z9--Lb-XF18_fRl_f6iAi5FrpwxrHVtzwTIhmropbCWS2ZAOsKYbfjGWWEJtcZRSZwQdgOGSUF7zbW2_AS9u-Pdz5sRrIGQJz2o_eRHPd2qqL16nAn-Wm3jjRKciSJTIXh1IJjizxlSVqNPSws6QJyTopKJhoki9b-hXRlO13YN_R8o57wXhBXoy787ePj6_RAL4O0dAIqONx4mlYyHYMD6CUxWNnpFiVo8o3Zq8YxaPKMIU8Uz_DfMerVZ</recordid><startdate>20160701</startdate><enddate>20160701</enddate><creator>Liu, Rong</creator><creator>Jin, J.-P.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20160701</creationdate><title>Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells</title><author>Liu, Rong ; Jin, J.-P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e385t-fcc26f6925e841ae985dd382ce8f022d43bfd5d01dcf180f55dbec28519a3aad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>actin</topic><topic>Actin cytoskeleton</topic><topic>Actin Cytoskeleton - metabolism</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Calponin isoform genes</topic><topic>Calponins</topic><topic>Cell Movement</topic><topic>embryogenesis</topic><topic>genes</topic><topic>Humans</topic><topic>Mechanoreceptors - metabolism</topic><topic>Mechanoregulation</topic><topic>Microfilament Proteins - genetics</topic><topic>microfilaments</topic><topic>Muscle Contraction - physiology</topic><topic>muscle development</topic><topic>muscle strength</topic><topic>myocytes</topic><topic>Myocytes, Smooth Muscle - metabolism</topic><topic>myosin</topic><topic>Myosins - metabolism</topic><topic>Non-muscle cell motility</topic><topic>Organ Specificity - genetics</topic><topic>phosphorylation</topic><topic>Protein Isoforms - genetics</topic><topic>regulatory proteins</topic><topic>Smooth muscle</topic><topic>Structure-Activity Relationship</topic><topic>structure-activity relationships</topic><topic>vertebrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Rong</creatorcontrib><creatorcontrib>Jin, J.-P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Rong</au><au>Jin, J.-P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>2016-07-01</date><risdate>2016</risdate><volume>585</volume><issue>1</issue><spage>143</spage><epage>153</epage><pages>143-153</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><abstract>Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. Three homologous genes, CNN1, CNN2 and CNN3, encoding calponin isoforms 1, 2, and 3, respectively, are present in vertebrate species. All three calponin isoforms are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton, while each isoform executes different physiological roles based on their cell type-specific expressions. Calponin 1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin 2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin 3 participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Phosphorylation has been extensively studied for the regulation of calponin functions. Cytoskeleton tension regulates the transcription of CNN2 gene and the degradation of calponin 2 protein. This review summarizes our knowledge learned from studies over the past three decades, focusing on the evolutionary lineage of calponin isoform genes, their tissue- and cell type-specific expressions, structure–function relationships, and mechanoregulation.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>26970176</pmid><doi>10.1016/j.gene.2016.02.040</doi><tpages>11</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0378-1119
ispartof Gene, 2016-07, Vol.585 (1), p.143-153
issn 0378-1119
1879-0038
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5325697
source MEDLINE; Elsevier ScienceDirect Journals
subjects actin
Actin cytoskeleton
Actin Cytoskeleton - metabolism
Calcium-Binding Proteins - genetics
Calponin isoform genes
Calponins
Cell Movement
embryogenesis
genes
Humans
Mechanoreceptors - metabolism
Mechanoregulation
Microfilament Proteins - genetics
microfilaments
Muscle Contraction - physiology
muscle development
muscle strength
myocytes
Myocytes, Smooth Muscle - metabolism
myosin
Myosins - metabolism
Non-muscle cell motility
Organ Specificity - genetics
phosphorylation
Protein Isoforms - genetics
regulatory proteins
Smooth muscle
Structure-Activity Relationship
structure-activity relationships
vertebrates
title Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T16%3A33%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Calponin%20isoforms%20CNN1,%20CNN2%20and%20CNN3:%20Regulators%20for%20actin%20cytoskeleton%20functions%20in%20smooth%20muscle%20and%20non-muscle%20cells&rft.jtitle=Gene&rft.au=Liu,%20Rong&rft.date=2016-07-01&rft.volume=585&rft.issue=1&rft.spage=143&rft.epage=153&rft.pages=143-153&rft.issn=0378-1119&rft.eissn=1879-0038&rft_id=info:doi/10.1016/j.gene.2016.02.040&rft_dat=%3Cproquest_pubme%3E1825425378%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1783339502&rft_id=info:pmid/26970176&rft_els_id=S0378111916301238&rfr_iscdi=true