Tyrosine phosphorylation‐dependence of caveolae‐mediated endocytosis
• Introduction • SRC signaling in caveolae‐mediated endocytosis • Potential role of SRC‐mediated phosphorylation of caveolin‐1 in caveolae‐mediated endocytosis • Role of actin cytoskeleton in caveolae‐mediated endocytosis • Conclusion Caveolae are flask‐shaped plasma membrane invaginations that...
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| Veröffentlicht in: | Journal of cellular and molecular medicine 2007-11, Vol.11 (6), p.1239-1250 |
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| creator | Sverdlov, Maria Shajahan, Ayesha N. Minshall, Richard D. |
| description | •
Introduction
•
SRC signaling in caveolae‐mediated endocytosis
•
Potential role of SRC‐mediated phosphorylation of caveolin‐1 in caveolae‐mediated endocytosis
•
Role of actin cytoskeleton in caveolae‐mediated endocytosis
•
Conclusion
Caveolae are flask‐shaped plasma membrane invaginations that mediate endocytosis and transcytosis of plasma macromolecules, such as albumin, insulin and low‐density lipoprotein (LDL), as well as certain viruses, bacteria and bacterial toxins. Caveolae‐mediated transcytosis of macromolecules is critical for maintaining vascular homeostasis by regulating the oncotic pressure gradient and tissue delivery of drugs, vitamins, lipids and ions. Entrapment of cargo within caveolae induces activation of signalling cascades leading to caveolae fission and internalization. Activation of Src tyrosine kinase is an early and essential step that triggers detachment of loaded caveolae from the plasma membrane. In this review, we examine how Srcmediated phosphorylation regulates caveolae‐mediated transport by orchestrating the localization and activity of essential proteins of the endocytic machinery to regulate caveolae formation and fission. |
| doi_str_mv | 10.1111/j.1582-4934.2007.00127.x |
| format | Article |
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Introduction
•
SRC signaling in caveolae‐mediated endocytosis
•
Potential role of SRC‐mediated phosphorylation of caveolin‐1 in caveolae‐mediated endocytosis
•
Role of actin cytoskeleton in caveolae‐mediated endocytosis
•
Conclusion
Caveolae are flask‐shaped plasma membrane invaginations that mediate endocytosis and transcytosis of plasma macromolecules, such as albumin, insulin and low‐density lipoprotein (LDL), as well as certain viruses, bacteria and bacterial toxins. Caveolae‐mediated transcytosis of macromolecules is critical for maintaining vascular homeostasis by regulating the oncotic pressure gradient and tissue delivery of drugs, vitamins, lipids and ions. Entrapment of cargo within caveolae induces activation of signalling cascades leading to caveolae fission and internalization. Activation of Src tyrosine kinase is an early and essential step that triggers detachment of loaded caveolae from the plasma membrane. In this review, we examine how Srcmediated phosphorylation regulates caveolae‐mediated transport by orchestrating the localization and activity of essential proteins of the endocytic machinery to regulate caveolae formation and fission.</description><identifier>ISSN: 1582-1838</identifier><identifier>EISSN: 1582-4934</identifier><identifier>DOI: 10.1111/j.1582-4934.2007.00127.x</identifier><identifier>PMID: 18205698</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Actin ; actin cytoskeleton ; Actins - metabolism ; Amino acids ; Animals ; Caveolae ; Caveolae - enzymology ; Caveolae - metabolism ; Caveolin-1 ; Cytoskeleton ; Cytoskeleton - metabolism ; Drug delivery ; Endocytosis ; Endothelium ; Homeostasis ; Humans ; Internalization ; Invaginations ; Kinases ; Lipids ; Localization ; Low density lipoprotein ; Macromolecules ; Membranes ; Microscopy ; Molecules ; Phosphorylation ; Phosphotyrosine - metabolism ; Physiology ; Plasma ; Protein transport ; Proteins ; Reviews ; Src ; src-Family Kinases - metabolism ; Toxins ; Vitamins</subject><ispartof>Journal of cellular and molecular medicine, 2007-11, Vol.11 (6), p.1239-1250</ispartof><rights>Copyright Blackwell Publishing Ltd. Nov/Dec 2007</rights><rights>2007. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4577-d603f902d00ef5e39f45c540ca8a4a7000e33cf33c7be0dcab626d952f84b0263</citedby><cites>FETCH-LOGICAL-c4577-d603f902d00ef5e39f45c540ca8a4a7000e33cf33c7be0dcab626d952f84b0263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401290/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401290/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,11541,27901,27902,45550,45551,46027,46451,53766,53768</link.rule.ids><linktorsrc>$$Uhttps://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1582-4934.2007.00127.x$$EView_record_in_Wiley-Blackwell$$FView_record_in_$$GWiley-Blackwell</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18205698$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sverdlov, Maria</creatorcontrib><creatorcontrib>Shajahan, Ayesha N.</creatorcontrib><creatorcontrib>Minshall, Richard D.</creatorcontrib><title>Tyrosine phosphorylation‐dependence of caveolae‐mediated endocytosis</title><title>Journal of cellular and molecular medicine</title><addtitle>J Cell Mol Med</addtitle><description>•
Introduction
•
SRC signaling in caveolae‐mediated endocytosis
•
Potential role of SRC‐mediated phosphorylation of caveolin‐1 in caveolae‐mediated endocytosis
•
Role of actin cytoskeleton in caveolae‐mediated endocytosis
•
Conclusion
Caveolae are flask‐shaped plasma membrane invaginations that mediate endocytosis and transcytosis of plasma macromolecules, such as albumin, insulin and low‐density lipoprotein (LDL), as well as certain viruses, bacteria and bacterial toxins. Caveolae‐mediated transcytosis of macromolecules is critical for maintaining vascular homeostasis by regulating the oncotic pressure gradient and tissue delivery of drugs, vitamins, lipids and ions. Entrapment of cargo within caveolae induces activation of signalling cascades leading to caveolae fission and internalization. Activation of Src tyrosine kinase is an early and essential step that triggers detachment of loaded caveolae from the plasma membrane. In this review, we examine how Srcmediated phosphorylation regulates caveolae‐mediated transport by orchestrating the localization and activity of essential proteins of the endocytic machinery to regulate caveolae formation and fission.</description><subject>Actin</subject><subject>actin cytoskeleton</subject><subject>Actins - metabolism</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Caveolae</subject><subject>Caveolae - enzymology</subject><subject>Caveolae - metabolism</subject><subject>Caveolin-1</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton - metabolism</subject><subject>Drug delivery</subject><subject>Endocytosis</subject><subject>Endothelium</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Internalization</subject><subject>Invaginations</subject><subject>Kinases</subject><subject>Lipids</subject><subject>Localization</subject><subject>Low density lipoprotein</subject><subject>Macromolecules</subject><subject>Membranes</subject><subject>Microscopy</subject><subject>Molecules</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine - metabolism</subject><subject>Physiology</subject><subject>Plasma</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Reviews</subject><subject>Src</subject><subject>src-Family Kinases - metabolism</subject><subject>Toxins</subject><subject>Vitamins</subject><issn>1582-1838</issn><issn>1582-4934</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNUdtu1DAQtRCIlsIvoAgk3jaMb7H9ABJaAQW14qU8W15nQrPKxkucLc1bP6HfyJcwYVflIiFha-SR58zRmTmMFRxKTufluuTaioVyUpUCwJQAXJjy-h47vivcP-TcSnvEHuW8BpAVl-4hO-JWgK6cPWanF9OQcttjsb1MmWKYujC2qf9-c1vjFvsa-4hFaooYrjB1AamwwboNI9YFlVOcRiLIj9mDJnQZnxzeE_b53duL5eni7NP7D8s3Z4uotDGLugLZOBA1ADYapWuUjlpBDDaoYIC-pYwNhVkh1DGsKlHVTovGqhWISp6w13ve7W5FOiL24xA6vx3aTRgmn0Lr_6z07aX_kq68UrQjB0Tw4kAwpK87zKPftDli14Ue0y570lAJa2fg87-A67QbehrOSzDKaGfcrOfZv1CCG7pWCwLZPSjSsvOAzZ1eDn521K_9bJafjfOzo_6no_6aWp_-Pu-vxoOFBHi1B3xrO5z-m9h_XJ6fUyZ_AD2ZsjI</recordid><startdate>200711</startdate><enddate>200711</enddate><creator>Sverdlov, Maria</creator><creator>Shajahan, Ayesha N.</creator><creator>Minshall, Richard D.</creator><general>Blackwell Publishing Ltd</general><general>John Wiley & Sons, Inc</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>K9.</scope><scope>3V.</scope><scope>7QP</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200711</creationdate><title>Tyrosine phosphorylation‐dependence of caveolae‐mediated endocytosis</title><author>Sverdlov, Maria ; Shajahan, Ayesha N. ; Minshall, Richard D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4577-d603f902d00ef5e39f45c540ca8a4a7000e33cf33c7be0dcab626d952f84b0263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Actin</topic><topic>actin cytoskeleton</topic><topic>Actins - metabolism</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Caveolae</topic><topic>Caveolae - enzymology</topic><topic>Caveolae - metabolism</topic><topic>Caveolin-1</topic><topic>Cytoskeleton</topic><topic>Cytoskeleton - metabolism</topic><topic>Drug delivery</topic><topic>Endocytosis</topic><topic>Endothelium</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Internalization</topic><topic>Invaginations</topic><topic>Kinases</topic><topic>Lipids</topic><topic>Localization</topic><topic>Low density lipoprotein</topic><topic>Macromolecules</topic><topic>Membranes</topic><topic>Microscopy</topic><topic>Molecules</topic><topic>Phosphorylation</topic><topic>Phosphotyrosine - metabolism</topic><topic>Physiology</topic><topic>Plasma</topic><topic>Protein transport</topic><topic>Proteins</topic><topic>Reviews</topic><topic>Src</topic><topic>src-Family Kinases - metabolism</topic><topic>Toxins</topic><topic>Vitamins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sverdlov, Maria</creatorcontrib><creatorcontrib>Shajahan, Ayesha N.</creatorcontrib><creatorcontrib>Minshall, Richard D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</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>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of cellular and molecular medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Sverdlov, Maria</au><au>Shajahan, Ayesha N.</au><au>Minshall, Richard D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tyrosine phosphorylation‐dependence of caveolae‐mediated endocytosis</atitle><jtitle>Journal of cellular and molecular medicine</jtitle><addtitle>J Cell Mol Med</addtitle><date>2007-11</date><risdate>2007</risdate><volume>11</volume><issue>6</issue><spage>1239</spage><epage>1250</epage><pages>1239-1250</pages><issn>1582-1838</issn><eissn>1582-4934</eissn><abstract>•
Introduction
•
SRC signaling in caveolae‐mediated endocytosis
•
Potential role of SRC‐mediated phosphorylation of caveolin‐1 in caveolae‐mediated endocytosis
•
Role of actin cytoskeleton in caveolae‐mediated endocytosis
•
Conclusion
Caveolae are flask‐shaped plasma membrane invaginations that mediate endocytosis and transcytosis of plasma macromolecules, such as albumin, insulin and low‐density lipoprotein (LDL), as well as certain viruses, bacteria and bacterial toxins. Caveolae‐mediated transcytosis of macromolecules is critical for maintaining vascular homeostasis by regulating the oncotic pressure gradient and tissue delivery of drugs, vitamins, lipids and ions. Entrapment of cargo within caveolae induces activation of signalling cascades leading to caveolae fission and internalization. Activation of Src tyrosine kinase is an early and essential step that triggers detachment of loaded caveolae from the plasma membrane. In this review, we examine how Srcmediated phosphorylation regulates caveolae‐mediated transport by orchestrating the localization and activity of essential proteins of the endocytic machinery to regulate caveolae formation and fission.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>18205698</pmid><doi>10.1111/j.1582-4934.2007.00127.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Actin actin cytoskeleton Actins - metabolism Amino acids Animals Caveolae Caveolae - enzymology Caveolae - metabolism Caveolin-1 Cytoskeleton Cytoskeleton - metabolism Drug delivery Endocytosis Endothelium Homeostasis Humans Internalization Invaginations Kinases Lipids Localization Low density lipoprotein Macromolecules Membranes Microscopy Molecules Phosphorylation Phosphotyrosine - metabolism Physiology Plasma Protein transport Proteins Reviews Src src-Family Kinases - metabolism Toxins Vitamins |
| title | Tyrosine phosphorylation‐dependence of caveolae‐mediated endocytosis |
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