A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes

Cell transformation by Rous sarcoma virus results in a dramatic change of adhesion structures with the substratum. Adhesion plaques are replaced by dot-like attachment sites called podosomes. Podosomes are also found constitutively in motile nontransformed cells such as leukocytes, macrophages, and...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Journal of cell biology 2000-07, Vol.150 (2), p.377-389
Hauptverfasser: Ochoa, Gian-Carlo, Slepnev, Vladimir I., Neff, Lynn, Ringstad, Niels, Takei, Kohji, Daniell, Laurie, Kim, Warren, Cao, Hong, McNiven, Mark, Baron, Roland, de Camilli, Pietro
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 389
container_issue 2
container_start_page 377
container_title The Journal of cell biology
container_volume 150
creator Ochoa, Gian-Carlo
Slepnev, Vladimir I.
Neff, Lynn
Ringstad, Niels
Takei, Kohji
Daniell, Laurie
Kim, Warren
Cao, Hong
McNiven, Mark
Baron, Roland
de Camilli, Pietro
description Cell transformation by Rous sarcoma virus results in a dramatic change of adhesion structures with the substratum. Adhesion plaques are replaced by dot-like attachment sites called podosomes. Podosomes are also found constitutively in motile nontransformed cells such as leukocytes, macrophages, and osteoclasts. They are represented by columnar arrays of actin which are perpendicular to the substratum and contain tubular invaginations of the plasma membrane. Given the similarity of these tubules to those generated by dynamin around a variety of membrane templates, we investigated whether dynamin is present at podosomes. Immunoreactivities for dynamin 2 and for the dynamin 2-binding protein endophilin 2 (SH3P8) were detected at podosomes of transformed cells and osteoclasts. Furthermore, GFP wild-type dynamin 2aa was targeted to podosomes. As shown by fluorescence recovery after photobleaching, GFP-dynamin 2aa and GFP-actin had a very rapid and similar turnover at podosomes. Expression of the GFP-dynamin 2 aaG273 Dabolished podosomes while GPF-dynaminK44 Awas targeted to podosomes but delayed actin turnover. These data demonstrate a functional link between a member of the dynamin family and actin at attachment sites between cells and the substratum.
doi_str_mv 10.1083/jcb.150.2.377
format Article
fullrecord <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2180219</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1619945</jstor_id><sourcerecordid>1619945</sourcerecordid><originalsourceid>FETCH-LOGICAL-c497t-e4d531352cacc6c29fada81b96d55896ea74ec17a4a84c5284fd677304efb8c93</originalsourceid><addsrcrecordid>eNpdkUtP3DAUha2qqExpl-yqymLBLlM_Y3tTaTRAQRqJLtq15Tg3JUNi09ihmn-P0aDyWN3F-XR0dD-EjilZUqL5t61vllSSJVtypd6hBZWCVJoK8h4tCGG0MpLJQ_QxpS0hRCjBP6BDSgzRUpkFulrhizn43MfgBrzpwy1uIP8DCPhsF9zYB-xCi_MN4FWhAl7vcky3MECOJcr4Z2xjiiOkT-igc0OCz0_3CP2-OP-1vqw21z-u1qtN5YVRuQLRSk65ZN55X3tmOtc6TRtTt1JqU4NTAjxVTjgtvGRadG2tFCcCukZ7w4_Q933v3dyM0HoIeXKDvZv60U07G11vXyehv7F_4r1lVJd_PBacPhVM8e8MKduxTx6GwQWIc7KKMlkLIwt48gbcxnkqf0qlSxHFjagLVO0hP8WUJuj-L6HEPhqyxZAthiyzxVDhv76c_4LeKynAlz2wTTlOz3lNjRGSPwDo7ZZD</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217073946</pqid></control><display><type>article</type><title>A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Ochoa, Gian-Carlo ; Slepnev, Vladimir I. ; Neff, Lynn ; Ringstad, Niels ; Takei, Kohji ; Daniell, Laurie ; Kim, Warren ; Cao, Hong ; McNiven, Mark ; Baron, Roland ; de Camilli, Pietro</creator><creatorcontrib>Ochoa, Gian-Carlo ; Slepnev, Vladimir I. ; Neff, Lynn ; Ringstad, Niels ; Takei, Kohji ; Daniell, Laurie ; Kim, Warren ; Cao, Hong ; McNiven, Mark ; Baron, Roland ; de Camilli, Pietro</creatorcontrib><description>Cell transformation by Rous sarcoma virus results in a dramatic change of adhesion structures with the substratum. Adhesion plaques are replaced by dot-like attachment sites called podosomes. Podosomes are also found constitutively in motile nontransformed cells such as leukocytes, macrophages, and osteoclasts. They are represented by columnar arrays of actin which are perpendicular to the substratum and contain tubular invaginations of the plasma membrane. Given the similarity of these tubules to those generated by dynamin around a variety of membrane templates, we investigated whether dynamin is present at podosomes. Immunoreactivities for dynamin 2 and for the dynamin 2-binding protein endophilin 2 (SH3P8) were detected at podosomes of transformed cells and osteoclasts. Furthermore, GFP wild-type dynamin 2aa was targeted to podosomes. As shown by fluorescence recovery after photobleaching, GFP-dynamin 2aa and GFP-actin had a very rapid and similar turnover at podosomes. Expression of the GFP-dynamin 2 aaG273 Dabolished podosomes while GPF-dynaminK44 Awas targeted to podosomes but delayed actin turnover. These data demonstrate a functional link between a member of the dynamin family and actin at attachment sites between cells and the substratum.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.150.2.377</identifier><identifier>PMID: 10908579</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Actins ; Actins - metabolism ; Antibodies ; Body Temperature - physiology ; Cell Adhesion - drug effects ; Cell Adhesion - physiology ; Cell Line, Transformed - drug effects ; Cell Line, Transformed - metabolism ; Cell Line, Transformed - ultrastructure ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Cell membranes ; Cells ; Cellular biology ; Cellular immunity ; Cyclosporine - pharmacology ; Cyclosporins ; Cytoskeleton - drug effects ; Cytoskeleton - metabolism ; Cytoskeleton - ultrastructure ; Dynamin I ; Dynamins ; Endocytosis ; Fluorescence ; GTP Phosphohydrolases - metabolism ; Microtubules - drug effects ; Microtubules - metabolism ; Microtubules - ultrastructure ; Mutation - physiology ; Neurons ; Original ; Osteoclasts ; Osteoclasts - drug effects ; Osteoclasts - metabolism ; Osteoclasts - ultrastructure ; Viruses</subject><ispartof>The Journal of cell biology, 2000-07, Vol.150 (2), p.377-389</ispartof><rights>Copyright 2000 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Jul 24, 2000</rights><rights>2000 The Rockefeller University Press 2000 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497t-e4d531352cacc6c29fada81b96d55896ea74ec17a4a84c5284fd677304efb8c93</citedby><cites>FETCH-LOGICAL-c497t-e4d531352cacc6c29fada81b96d55896ea74ec17a4a84c5284fd677304efb8c93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10908579$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ochoa, Gian-Carlo</creatorcontrib><creatorcontrib>Slepnev, Vladimir I.</creatorcontrib><creatorcontrib>Neff, Lynn</creatorcontrib><creatorcontrib>Ringstad, Niels</creatorcontrib><creatorcontrib>Takei, Kohji</creatorcontrib><creatorcontrib>Daniell, Laurie</creatorcontrib><creatorcontrib>Kim, Warren</creatorcontrib><creatorcontrib>Cao, Hong</creatorcontrib><creatorcontrib>McNiven, Mark</creatorcontrib><creatorcontrib>Baron, Roland</creatorcontrib><creatorcontrib>de Camilli, Pietro</creatorcontrib><title>A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Cell transformation by Rous sarcoma virus results in a dramatic change of adhesion structures with the substratum. Adhesion plaques are replaced by dot-like attachment sites called podosomes. Podosomes are also found constitutively in motile nontransformed cells such as leukocytes, macrophages, and osteoclasts. They are represented by columnar arrays of actin which are perpendicular to the substratum and contain tubular invaginations of the plasma membrane. Given the similarity of these tubules to those generated by dynamin around a variety of membrane templates, we investigated whether dynamin is present at podosomes. Immunoreactivities for dynamin 2 and for the dynamin 2-binding protein endophilin 2 (SH3P8) were detected at podosomes of transformed cells and osteoclasts. Furthermore, GFP wild-type dynamin 2aa was targeted to podosomes. As shown by fluorescence recovery after photobleaching, GFP-dynamin 2aa and GFP-actin had a very rapid and similar turnover at podosomes. Expression of the GFP-dynamin 2 aaG273 Dabolished podosomes while GPF-dynaminK44 Awas targeted to podosomes but delayed actin turnover. These data demonstrate a functional link between a member of the dynamin family and actin at attachment sites between cells and the substratum.</description><subject>Actins</subject><subject>Actins - metabolism</subject><subject>Antibodies</subject><subject>Body Temperature - physiology</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Line, Transformed - drug effects</subject><subject>Cell Line, Transformed - metabolism</subject><subject>Cell Line, Transformed - ultrastructure</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - ultrastructure</subject><subject>Cell membranes</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Cellular immunity</subject><subject>Cyclosporine - pharmacology</subject><subject>Cyclosporins</subject><subject>Cytoskeleton - drug effects</subject><subject>Cytoskeleton - metabolism</subject><subject>Cytoskeleton - ultrastructure</subject><subject>Dynamin I</subject><subject>Dynamins</subject><subject>Endocytosis</subject><subject>Fluorescence</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>Microtubules - drug effects</subject><subject>Microtubules - metabolism</subject><subject>Microtubules - ultrastructure</subject><subject>Mutation - physiology</subject><subject>Neurons</subject><subject>Original</subject><subject>Osteoclasts</subject><subject>Osteoclasts - drug effects</subject><subject>Osteoclasts - metabolism</subject><subject>Osteoclasts - ultrastructure</subject><subject>Viruses</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtP3DAUha2qqExpl-yqymLBLlM_Y3tTaTRAQRqJLtq15Tg3JUNi09ihmn-P0aDyWN3F-XR0dD-EjilZUqL5t61vllSSJVtypd6hBZWCVJoK8h4tCGG0MpLJQ_QxpS0hRCjBP6BDSgzRUpkFulrhizn43MfgBrzpwy1uIP8DCPhsF9zYB-xCi_MN4FWhAl7vcky3MECOJcr4Z2xjiiOkT-igc0OCz0_3CP2-OP-1vqw21z-u1qtN5YVRuQLRSk65ZN55X3tmOtc6TRtTt1JqU4NTAjxVTjgtvGRadG2tFCcCukZ7w4_Q933v3dyM0HoIeXKDvZv60U07G11vXyehv7F_4r1lVJd_PBacPhVM8e8MKduxTx6GwQWIc7KKMlkLIwt48gbcxnkqf0qlSxHFjagLVO0hP8WUJuj-L6HEPhqyxZAthiyzxVDhv76c_4LeKynAlz2wTTlOz3lNjRGSPwDo7ZZD</recordid><startdate>20000724</startdate><enddate>20000724</enddate><creator>Ochoa, Gian-Carlo</creator><creator>Slepnev, Vladimir I.</creator><creator>Neff, Lynn</creator><creator>Ringstad, Niels</creator><creator>Takei, Kohji</creator><creator>Daniell, Laurie</creator><creator>Kim, Warren</creator><creator>Cao, Hong</creator><creator>McNiven, Mark</creator><creator>Baron, Roland</creator><creator>de Camilli, Pietro</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000724</creationdate><title>A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes</title><author>Ochoa, Gian-Carlo ; Slepnev, Vladimir I. ; Neff, Lynn ; Ringstad, Niels ; Takei, Kohji ; Daniell, Laurie ; Kim, Warren ; Cao, Hong ; McNiven, Mark ; Baron, Roland ; de Camilli, Pietro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-e4d531352cacc6c29fada81b96d55896ea74ec17a4a84c5284fd677304efb8c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Actins</topic><topic>Actins - metabolism</topic><topic>Antibodies</topic><topic>Body Temperature - physiology</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Line, Transformed - drug effects</topic><topic>Cell Line, Transformed - metabolism</topic><topic>Cell Line, Transformed - ultrastructure</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - ultrastructure</topic><topic>Cell membranes</topic><topic>Cells</topic><topic>Cellular biology</topic><topic>Cellular immunity</topic><topic>Cyclosporine - pharmacology</topic><topic>Cyclosporins</topic><topic>Cytoskeleton - drug effects</topic><topic>Cytoskeleton - metabolism</topic><topic>Cytoskeleton - ultrastructure</topic><topic>Dynamin I</topic><topic>Dynamins</topic><topic>Endocytosis</topic><topic>Fluorescence</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>Microtubules - drug effects</topic><topic>Microtubules - metabolism</topic><topic>Microtubules - ultrastructure</topic><topic>Mutation - physiology</topic><topic>Neurons</topic><topic>Original</topic><topic>Osteoclasts</topic><topic>Osteoclasts - drug effects</topic><topic>Osteoclasts - metabolism</topic><topic>Osteoclasts - ultrastructure</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ochoa, Gian-Carlo</creatorcontrib><creatorcontrib>Slepnev, Vladimir I.</creatorcontrib><creatorcontrib>Neff, Lynn</creatorcontrib><creatorcontrib>Ringstad, Niels</creatorcontrib><creatorcontrib>Takei, Kohji</creatorcontrib><creatorcontrib>Daniell, Laurie</creatorcontrib><creatorcontrib>Kim, Warren</creatorcontrib><creatorcontrib>Cao, Hong</creatorcontrib><creatorcontrib>McNiven, Mark</creatorcontrib><creatorcontrib>Baron, Roland</creatorcontrib><creatorcontrib>de Camilli, Pietro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ochoa, Gian-Carlo</au><au>Slepnev, Vladimir I.</au><au>Neff, Lynn</au><au>Ringstad, Niels</au><au>Takei, Kohji</au><au>Daniell, Laurie</au><au>Kim, Warren</au><au>Cao, Hong</au><au>McNiven, Mark</au><au>Baron, Roland</au><au>de Camilli, Pietro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2000-07-24</date><risdate>2000</risdate><volume>150</volume><issue>2</issue><spage>377</spage><epage>389</epage><pages>377-389</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Cell transformation by Rous sarcoma virus results in a dramatic change of adhesion structures with the substratum. Adhesion plaques are replaced by dot-like attachment sites called podosomes. Podosomes are also found constitutively in motile nontransformed cells such as leukocytes, macrophages, and osteoclasts. They are represented by columnar arrays of actin which are perpendicular to the substratum and contain tubular invaginations of the plasma membrane. Given the similarity of these tubules to those generated by dynamin around a variety of membrane templates, we investigated whether dynamin is present at podosomes. Immunoreactivities for dynamin 2 and for the dynamin 2-binding protein endophilin 2 (SH3P8) were detected at podosomes of transformed cells and osteoclasts. Furthermore, GFP wild-type dynamin 2aa was targeted to podosomes. As shown by fluorescence recovery after photobleaching, GFP-dynamin 2aa and GFP-actin had a very rapid and similar turnover at podosomes. Expression of the GFP-dynamin 2 aaG273 Dabolished podosomes while GPF-dynaminK44 Awas targeted to podosomes but delayed actin turnover. These data demonstrate a functional link between a member of the dynamin family and actin at attachment sites between cells and the substratum.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>10908579</pmid><doi>10.1083/jcb.150.2.377</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9525
ispartof The Journal of cell biology, 2000-07, Vol.150 (2), p.377-389
issn 0021-9525
1540-8140
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2180219
source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Actins
Actins - metabolism
Antibodies
Body Temperature - physiology
Cell Adhesion - drug effects
Cell Adhesion - physiology
Cell Line, Transformed - drug effects
Cell Line, Transformed - metabolism
Cell Line, Transformed - ultrastructure
Cell Membrane - drug effects
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Cell membranes
Cells
Cellular biology
Cellular immunity
Cyclosporine - pharmacology
Cyclosporins
Cytoskeleton - drug effects
Cytoskeleton - metabolism
Cytoskeleton - ultrastructure
Dynamin I
Dynamins
Endocytosis
Fluorescence
GTP Phosphohydrolases - metabolism
Microtubules - drug effects
Microtubules - metabolism
Microtubules - ultrastructure
Mutation - physiology
Neurons
Original
Osteoclasts
Osteoclasts - drug effects
Osteoclasts - metabolism
Osteoclasts - ultrastructure
Viruses
title A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T06%3A03%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20Functional%20Link%20between%20Dynamin%20and%20the%20Actin%20Cytoskeleton%20at%20Podosomes&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Ochoa,%20Gian-Carlo&rft.date=2000-07-24&rft.volume=150&rft.issue=2&rft.spage=377&rft.epage=389&rft.pages=377-389&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.150.2.377&rft_dat=%3Cjstor_pubme%3E1619945%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217073946&rft_id=info:pmid/10908579&rft_jstor_id=1619945&rfr_iscdi=true