Src regulates membrane trafficking of the Kv3.1b channel
•Src inhibits Kv3.1b trafficking to the plasma membrane.•Src induces a dramatic redistribution of Kv3.1b to the endoplasmic reticulum.•Src decreases the peak current densities of the Kv3.1b channel.•Src alters the steady-state inactivation of the kv3.1b channel. The Kv3.1 channel plays a crucial rol...
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| Veröffentlicht in: | FEBS letters 2014-01, Vol.588 (1), p.86-91 |
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| creator | Bae, Seong Han Kim, Dong Hyun Shin, Seok Kyo Choi, Jin Sung Park, Kang-Sik |
| description | •Src inhibits Kv3.1b trafficking to the plasma membrane.•Src induces a dramatic redistribution of Kv3.1b to the endoplasmic reticulum.•Src decreases the peak current densities of the Kv3.1b channel.•Src alters the steady-state inactivation of the kv3.1b channel.
The Kv3.1 channel plays a crucial role in regulating the high-frequency firing properties of neurons. Here, we determined whether Src regulates the subcellular distributions of the Kv3.1b channel. Co-expression of active Src induced a dramatic redistribution of Kv3.1b to the endoplasmic reticulum. Furthermore, co-expression of the Kv3.1b channel with active Src induced a remarkable decrease in the pool of Kv3.1b at the cell surface. Moreover, the co-expression of active Src results in a significant decrease in the peak current densities of the Kv3.1b channel, and a substantial alteration in the voltage dependence of its steady-state inactivation. Taken together, these results indicate that Src kinase may play an important role in regulating membrane trafficking of Kv3.1b channels. |
| doi_str_mv | 10.1016/j.febslet.2013.11.010 |
| format | Article |
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The Kv3.1 channel plays a crucial role in regulating the high-frequency firing properties of neurons. Here, we determined whether Src regulates the subcellular distributions of the Kv3.1b channel. Co-expression of active Src induced a dramatic redistribution of Kv3.1b to the endoplasmic reticulum. Furthermore, co-expression of the Kv3.1b channel with active Src induced a remarkable decrease in the pool of Kv3.1b at the cell surface. Moreover, the co-expression of active Src results in a significant decrease in the peak current densities of the Kv3.1b channel, and a substantial alteration in the voltage dependence of its steady-state inactivation. Taken together, these results indicate that Src kinase may play an important role in regulating membrane trafficking of Kv3.1b channels.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2013.11.010</identifier><identifier>PMID: 24291260</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Blotting, Western ; Cell Membrane - metabolism ; Cell Membrane - physiology ; Chlorocebus aethiops ; COS Cells ; Endoplasmic Reticulum - metabolism ; HEK293 Cells ; Humans ; Kv3.1b ; Membrane Potentials - physiology ; Membrane trafficking ; Mice ; Mutagenesis, Site-Directed ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Nerve Tissue Proteins - physiology ; Patch-Clamp Techniques ; Potassium channel ; Protein Transport ; Proto-Oncogene Proteins pp60(c-src) - genetics ; Proto-Oncogene Proteins pp60(c-src) - metabolism ; Rats ; Shaw Potassium Channels - genetics ; Shaw Potassium Channels - metabolism ; Shaw Potassium Channels - physiology ; Src</subject><ispartof>FEBS letters, 2014-01, Vol.588 (1), p.86-91</ispartof><rights>2013 Federation of European Biochemical Societies</rights><rights>FEBS Letters 588 (2014) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4772-6b33a179e850aeb9121cb02de5481c22d1a74d08def2c204837a79e54fa6127e3</citedby><cites>FETCH-LOGICAL-c4772-6b33a179e850aeb9121cb02de5481c22d1a74d08def2c204837a79e54fa6127e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2013.11.010$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2013.11.010$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24291260$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bae, Seong Han</creatorcontrib><creatorcontrib>Kim, Dong Hyun</creatorcontrib><creatorcontrib>Shin, Seok Kyo</creatorcontrib><creatorcontrib>Choi, Jin Sung</creatorcontrib><creatorcontrib>Park, Kang-Sik</creatorcontrib><title>Src regulates membrane trafficking of the Kv3.1b channel</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>•Src inhibits Kv3.1b trafficking to the plasma membrane.•Src induces a dramatic redistribution of Kv3.1b to the endoplasmic reticulum.•Src decreases the peak current densities of the Kv3.1b channel.•Src alters the steady-state inactivation of the kv3.1b channel.
The Kv3.1 channel plays a crucial role in regulating the high-frequency firing properties of neurons. Here, we determined whether Src regulates the subcellular distributions of the Kv3.1b channel. Co-expression of active Src induced a dramatic redistribution of Kv3.1b to the endoplasmic reticulum. Furthermore, co-expression of the Kv3.1b channel with active Src induced a remarkable decrease in the pool of Kv3.1b at the cell surface. Moreover, the co-expression of active Src results in a significant decrease in the peak current densities of the Kv3.1b channel, and a substantial alteration in the voltage dependence of its steady-state inactivation. Taken together, these results indicate that Src kinase may play an important role in regulating membrane trafficking of Kv3.1b channels.</description><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - physiology</subject><subject>Chlorocebus aethiops</subject><subject>COS Cells</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Kv3.1b</subject><subject>Membrane Potentials - physiology</subject><subject>Membrane trafficking</subject><subject>Mice</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Patch-Clamp Techniques</subject><subject>Potassium channel</subject><subject>Protein Transport</subject><subject>Proto-Oncogene Proteins pp60(c-src) - genetics</subject><subject>Proto-Oncogene Proteins pp60(c-src) - metabolism</subject><subject>Rats</subject><subject>Shaw Potassium Channels - genetics</subject><subject>Shaw Potassium Channels - metabolism</subject><subject>Shaw Potassium Channels - physiology</subject><subject>Src</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtP3TAQha2KqlygP6FVlmwSZmwndlYIEC8ViQWwthxnAr7Ng9q5VPz7OrqXbtvVaKQz5xx9w9g3hAIBq5N10VETe5oLDigKxAIQPrEVaiVyISu9x1YAKPNS1WKfHcS4hrRrrL-wfS55jbyCFdMPwWWBnje9nSlmAw1NsCNlc7Bd591PPz5nU5fNL5T9eEsxTeZe7DhSf8Q-d7aP9HU3D9nT1eXjxU1-d399e3F2lzupFM-rRgiLqiZdgqUmpaJrgLdUSo2O8xatki3oljruOEgtlE3qUna2Qq5IHLLjre9rmH5tKM5m8NFR36eW0yYalDUoDQJ5kpZbqQtTjIE68xr8YMO7QTALNLM2O2hmgWYQTYKW7r7vIjbNQO3fqw9KSXCzFfz2Pb3_n6u5ujznD8sHlgegANBSLh1Pt1aUmL15CiY6T6Oj1gdys2kn_4-2fwB8aJNH</recordid><startdate>20140103</startdate><enddate>20140103</enddate><creator>Bae, Seong Han</creator><creator>Kim, Dong Hyun</creator><creator>Shin, Seok Kyo</creator><creator>Choi, Jin Sung</creator><creator>Park, Kang-Sik</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>20140103</creationdate><title>Src regulates membrane trafficking of the Kv3.1b channel</title><author>Bae, Seong Han ; Kim, Dong Hyun ; Shin, Seok Kyo ; Choi, Jin Sung ; Park, Kang-Sik</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4772-6b33a179e850aeb9121cb02de5481c22d1a74d08def2c204837a79e54fa6127e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - physiology</topic><topic>Chlorocebus aethiops</topic><topic>COS Cells</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Kv3.1b</topic><topic>Membrane Potentials - physiology</topic><topic>Membrane trafficking</topic><topic>Mice</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Patch-Clamp Techniques</topic><topic>Potassium channel</topic><topic>Protein Transport</topic><topic>Proto-Oncogene Proteins pp60(c-src) - genetics</topic><topic>Proto-Oncogene Proteins pp60(c-src) - metabolism</topic><topic>Rats</topic><topic>Shaw Potassium Channels - genetics</topic><topic>Shaw Potassium Channels - metabolism</topic><topic>Shaw Potassium Channels - physiology</topic><topic>Src</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bae, Seong Han</creatorcontrib><creatorcontrib>Kim, Dong Hyun</creatorcontrib><creatorcontrib>Shin, Seok Kyo</creatorcontrib><creatorcontrib>Choi, Jin Sung</creatorcontrib><creatorcontrib>Park, Kang-Sik</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bae, Seong Han</au><au>Kim, Dong Hyun</au><au>Shin, Seok Kyo</au><au>Choi, Jin Sung</au><au>Park, Kang-Sik</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Src regulates membrane trafficking of the Kv3.1b channel</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2014-01-03</date><risdate>2014</risdate><volume>588</volume><issue>1</issue><spage>86</spage><epage>91</epage><pages>86-91</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•Src inhibits Kv3.1b trafficking to the plasma membrane.•Src induces a dramatic redistribution of Kv3.1b to the endoplasmic reticulum.•Src decreases the peak current densities of the Kv3.1b channel.•Src alters the steady-state inactivation of the kv3.1b channel.
The Kv3.1 channel plays a crucial role in regulating the high-frequency firing properties of neurons. Here, we determined whether Src regulates the subcellular distributions of the Kv3.1b channel. Co-expression of active Src induced a dramatic redistribution of Kv3.1b to the endoplasmic reticulum. Furthermore, co-expression of the Kv3.1b channel with active Src induced a remarkable decrease in the pool of Kv3.1b at the cell surface. Moreover, the co-expression of active Src results in a significant decrease in the peak current densities of the Kv3.1b channel, and a substantial alteration in the voltage dependence of its steady-state inactivation. Taken together, these results indicate that Src kinase may play an important role in regulating membrane trafficking of Kv3.1b channels.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>24291260</pmid><doi>10.1016/j.febslet.2013.11.010</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Blotting, Western Cell Membrane - metabolism Cell Membrane - physiology Chlorocebus aethiops COS Cells Endoplasmic Reticulum - metabolism HEK293 Cells Humans Kv3.1b Membrane Potentials - physiology Membrane trafficking Mice Mutagenesis, Site-Directed Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - physiology Patch-Clamp Techniques Potassium channel Protein Transport Proto-Oncogene Proteins pp60(c-src) - genetics Proto-Oncogene Proteins pp60(c-src) - metabolism Rats Shaw Potassium Channels - genetics Shaw Potassium Channels - metabolism Shaw Potassium Channels - physiology Src |
| title | Src regulates membrane trafficking of the Kv3.1b channel |
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