Ca2+/calmodulin binds and dissociates K-RasB from membrane
We have investigated the interaction of calmodulin (CaM) with Ras-p21 and the significance of this association. All Ras-p21 isoforms tested (H-, K-, and N-Ras) were detected in the particulate fraction of human platelets and MCF-7 cells, a human breast cancer cell line. In MCF-7 cells, H- and N-Ras...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2003-05, Vol.304 (4), p.655-660 |
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| creator | Sidhu, Ranjinder S Clough, Richard R Bhullar, Rajinder P |
| description | We have investigated the interaction of calmodulin (CaM) with Ras-p21 and the significance of this association. All Ras-p21 isoforms tested (H-, K-, and N-Ras) were detected in the particulate fraction of human platelets and MCF-7 cells, a human breast cancer cell line. In MCF-7 cells, H- and N-Ras were also detected in the cytosolic fraction. K-RasB from platelet and MCF-7 cell lysates was found to bind CaM in a Ca2+ -dependent but GTPgammaS-independent manner. The yeast two-hybrid analysis demonstrated that K-RasB binds to CaM in vivo. Incubation of isolated membranes from platelet and MCF-7 cells with CaM caused dissociation of only K-RasB from membranes in a Ca2+ -dependent manner. CaM antagonist, W7, inhibited dissociation of K-RasB. Addition of platelet or MCF-7 cytosol alone to isolated platelet membranes did not cause dissociation of K-RasB and only addition of exogenous CaM caused dissociation. The results suggest a potential role for Ca2+/CaM in the regulation of K-RasB function. |
| doi_str_mv | 10.1016/S0006-291X(03)00635-1 |
| format | Article |
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All Ras-p21 isoforms tested (H-, K-, and N-Ras) were detected in the particulate fraction of human platelets and MCF-7 cells, a human breast cancer cell line. In MCF-7 cells, H- and N-Ras were also detected in the cytosolic fraction. K-RasB from platelet and MCF-7 cell lysates was found to bind CaM in a Ca2+ -dependent but GTPgammaS-independent manner. The yeast two-hybrid analysis demonstrated that K-RasB binds to CaM in vivo. Incubation of isolated membranes from platelet and MCF-7 cells with CaM caused dissociation of only K-RasB from membranes in a Ca2+ -dependent manner. CaM antagonist, W7, inhibited dissociation of K-RasB. Addition of platelet or MCF-7 cytosol alone to isolated platelet membranes did not cause dissociation of K-RasB and only addition of exogenous CaM caused dissociation. The results suggest a potential role for Ca2+/CaM in the regulation of K-RasB function.</description><subject>Blood Platelets - metabolism</subject><subject>Calcium - metabolism</subject><subject>Calmodulin - metabolism</subject><subject>Cell Fractionation</subject><subject>Cell Membrane - metabolism</subject><subject>Genes, ras</subject><subject>Guanosine 5'-O-(3-Thiotriphosphate) - metabolism</subject><subject>Humans</subject><subject>Protein Binding</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Proto-Oncogene Proteins p21(ras) - genetics</subject><subject>Proto-Oncogene Proteins p21(ras) - metabolism</subject><subject>Tumor Cells, Cultured</subject><subject>Two-Hybrid System Techniques</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkFtLxDAQhfOguOvqT1D6JIrUnUnatPFNF2-4IHgB30KaC1Sadk3aB_-93QvKPMwwnDNz-Ag5QbhCQD5_AwCeUoGf58AuxpnlKe6R6d96Qg5j_AJAzLg4IBOkxViQTcn1QtHLuVaN78zQ1G1S1a2JiWpNYuoYO12r3sbkOX1V8TZxofOJt74KqrVHZN-pJtrjXZ-Rj_u798Vjunx5eFrcLFNNWdGnuuRGG54pw5hSuS4ryoCjFZXT3BpncqHROizHRC5DbkpEsHkhTGYsFzmbkbPt3VXovgcbe-nrqG3TjBm6IcqCUU6hFKMw3wp16GIM1slVqL0KPxJBrkHJDSi5JiKByQ0oiaPvdPdgqLw1_64dJfYL-GBlBw</recordid><startdate>20030516</startdate><enddate>20030516</enddate><creator>Sidhu, Ranjinder S</creator><creator>Clough, Richard R</creator><creator>Bhullar, Rajinder P</creator><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>20030516</creationdate><title>Ca2+/calmodulin binds and dissociates K-RasB from membrane</title><author>Sidhu, Ranjinder S ; Clough, Richard R ; Bhullar, Rajinder P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c237t-c86dcd64ad33aa5c8b23061e9bfc6edfd59c1ef18272f416d8110e579d4de6953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Blood Platelets - metabolism</topic><topic>Calcium - metabolism</topic><topic>Calmodulin - metabolism</topic><topic>Cell Fractionation</topic><topic>Cell Membrane - metabolism</topic><topic>Genes, ras</topic><topic>Guanosine 5'-O-(3-Thiotriphosphate) - metabolism</topic><topic>Humans</topic><topic>Protein Binding</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Proto-Oncogene Proteins p21(ras) - genetics</topic><topic>Proto-Oncogene Proteins p21(ras) - metabolism</topic><topic>Tumor Cells, Cultured</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sidhu, Ranjinder S</creatorcontrib><creatorcontrib>Clough, Richard R</creatorcontrib><creatorcontrib>Bhullar, Rajinder P</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sidhu, Ranjinder S</au><au>Clough, Richard R</au><au>Bhullar, Rajinder P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ca2+/calmodulin binds and dissociates K-RasB from membrane</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2003-05-16</date><risdate>2003</risdate><volume>304</volume><issue>4</issue><spage>655</spage><epage>660</epage><pages>655-660</pages><issn>0006-291X</issn><abstract>We have investigated the interaction of calmodulin (CaM) with Ras-p21 and the significance of this association. All Ras-p21 isoforms tested (H-, K-, and N-Ras) were detected in the particulate fraction of human platelets and MCF-7 cells, a human breast cancer cell line. In MCF-7 cells, H- and N-Ras were also detected in the cytosolic fraction. K-RasB from platelet and MCF-7 cell lysates was found to bind CaM in a Ca2+ -dependent but GTPgammaS-independent manner. The yeast two-hybrid analysis demonstrated that K-RasB binds to CaM in vivo. Incubation of isolated membranes from platelet and MCF-7 cells with CaM caused dissociation of only K-RasB from membranes in a Ca2+ -dependent manner. CaM antagonist, W7, inhibited dissociation of K-RasB. Addition of platelet or MCF-7 cytosol alone to isolated platelet membranes did not cause dissociation of K-RasB and only addition of exogenous CaM caused dissociation. The results suggest a potential role for Ca2+/CaM in the regulation of K-RasB function.</abstract><cop>United States</cop><pmid>12727204</pmid><doi>10.1016/S0006-291X(03)00635-1</doi><tpages>6</tpages></addata></record> |
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| subjects | Blood Platelets - metabolism Calcium - metabolism Calmodulin - metabolism Cell Fractionation Cell Membrane - metabolism Genes, ras Guanosine 5'-O-(3-Thiotriphosphate) - metabolism Humans Protein Binding Protein Isoforms - genetics Protein Isoforms - metabolism Proto-Oncogene Proteins p21(ras) - genetics Proto-Oncogene Proteins p21(ras) - metabolism Tumor Cells, Cultured Two-Hybrid System Techniques |
| title | Ca2+/calmodulin binds and dissociates K-RasB from membrane |
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