Molecular determinants of Rem2 regulation of N-type calcium channels
Rem2 belongs to the RGK family of small GTPases whose members are known to interact with the voltage gated calcium channel β subunit, and to inhibit or abolish calcium currents. To identify the underlying functional domains of Rem2, we created several N- or C-terminally truncated Rem2 proteins and e...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2008-04, Vol.368 (3), p.827-831 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Flynn, Robyn Chen, Lina Hameed, Shahid Spafford, J. David Zamponi, Gerald W. |
| description | Rem2 belongs to the RGK family of small GTPases whose members are known to interact with the voltage gated calcium channel β subunit, and to inhibit or abolish calcium currents. To identify the underlying functional domains of Rem2, we created several N- or C-terminally truncated Rem2 proteins and examined their abilities to interact with the Cav β subunit and to regulate the activities of Cav2.2 N-type calcium channels. Confocal imaging of Rem2 in tsA-201 cells revealed that it contains a membrane-targeting signal in its C-terminus, consistent with previous studies. Co-precipitation assays showed that Cav β3 interaction depends on Rem2 residues 1–123. Only Rem2 proteins that targeted the cell membrane as well as bound the β subunit were able to reduce whole cell calcium currents. |
| doi_str_mv | 10.1016/j.bbrc.2008.02.020 |
| format | Article |
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Only Rem2 proteins that targeted the cell membrane as well as bound the β subunit were able to reduce whole cell calcium currents.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2008.02.020</identifier><identifier>PMID: 18279668</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Beta subunit ; Calcium - metabolism ; Calcium channel ; Calcium Channels, N-Type - chemistry ; Calcium Channels, N-Type - metabolism ; Cell Line ; GTPase ; Humans ; Ion Channel Gating - physiology ; Kidney - metabolism ; Mice ; Monomeric GTP-Binding Proteins - chemistry ; Monomeric GTP-Binding Proteins - metabolism ; Rem2 ; RGK protein ; Structure-Activity Relationship</subject><ispartof>Biochemical and biophysical research communications, 2008-04, Vol.368 (3), p.827-831</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-965e89e3d59f01a52a5ee0027e72d3b63863b8a0f9ae050e00cc7d279a09554f3</citedby><cites>FETCH-LOGICAL-c385t-965e89e3d59f01a52a5ee0027e72d3b63863b8a0f9ae050e00cc7d279a09554f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X08002507$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18279668$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Flynn, Robyn</creatorcontrib><creatorcontrib>Chen, Lina</creatorcontrib><creatorcontrib>Hameed, Shahid</creatorcontrib><creatorcontrib>Spafford, J. 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Only Rem2 proteins that targeted the cell membrane as well as bound the β subunit were able to reduce whole cell calcium currents.</description><subject>Animals</subject><subject>Beta subunit</subject><subject>Calcium - metabolism</subject><subject>Calcium channel</subject><subject>Calcium Channels, N-Type - chemistry</subject><subject>Calcium Channels, N-Type - metabolism</subject><subject>Cell Line</subject><subject>GTPase</subject><subject>Humans</subject><subject>Ion Channel Gating - physiology</subject><subject>Kidney - metabolism</subject><subject>Mice</subject><subject>Monomeric GTP-Binding Proteins - chemistry</subject><subject>Monomeric GTP-Binding Proteins - metabolism</subject><subject>Rem2</subject><subject>RGK protein</subject><subject>Structure-Activity Relationship</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMo7rr6BzxIT95aJ8k2bcCLrJ-wKoiCt5CmU83SjzVphf33puyCN4WBgZlnXoaHkFMKCQUqLlZJUTiTMIA8ARYK9siUgoSYUZjvkykAiJhJ-j4hR96vACidC3lIJjRnmRQin5Lrx65GM9TaRSX26Brb6rb3UVdFL9iwyOFHWPa2a8fRU9xv1hgZXRs7NJH51G2LtT8mB5WuPZ7s-oy83d68Lu7j5fPdw-JqGRuep30sRYq5RF6msgKqU6ZTRACWYcZKXgieC17kGiqpEVIIK2OyMnyqQabpvOIzcr7NXbvua0Dfq8Z6g3WtW-wGrzLggtGM_gsyEMAzEAFkW9C4znuHlVo722i3URTUKFmt1ChZjZIVsFAQjs526UPRYPl7srMagMstENzgt0WnvLHYGiytQ9OrsrN_5f8AmDyMXQ</recordid><startdate>20080411</startdate><enddate>20080411</enddate><creator>Flynn, Robyn</creator><creator>Chen, Lina</creator><creator>Hameed, Shahid</creator><creator>Spafford, J. 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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Beta subunit Calcium - metabolism Calcium channel Calcium Channels, N-Type - chemistry Calcium Channels, N-Type - metabolism Cell Line GTPase Humans Ion Channel Gating - physiology Kidney - metabolism Mice Monomeric GTP-Binding Proteins - chemistry Monomeric GTP-Binding Proteins - metabolism Rem2 RGK protein Structure-Activity Relationship |
| title | Molecular determinants of Rem2 regulation of N-type calcium channels |
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