The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme
Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518–803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2α) under non-stressed conditions. A K D of 4×10 −7 was determined for this binding. Heparin competed with Grp94-CT...
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| Veröffentlicht in: | FEBS letters 2001-09, Vol.505 (1), p.42-46 |
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| creator | Roher, Nerea Sarno, Stefania Miró, Francesc Ruzzene, Maria Llorens, Franc Meggio, Flavio Itarte, Emilio Pinna, Lorenzo A Plana, Maria |
| description | Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518–803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2α) under non-stressed conditions. A
K
D of 4×10
−7 was determined for this binding. Heparin competed with Grp94-CT for binding to CK2α. CK2β also inhibited the binding of Grp94-CT to CK2α, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2α mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74–77) present in helix C of CK2α. Grp94-CT stimulated the activity of CK2α wild-type but was ineffective on the CK2α K74–77A mutant. |
| doi_str_mv | 10.1016/S0014-5793(01)02781-8 |
| format | Article |
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K
D of 4×10
−7 was determined for this binding. Heparin competed with Grp94-CT for binding to CK2α. CK2β also inhibited the binding of Grp94-CT to CK2α, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2α mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74–77) present in helix C of CK2α. Grp94-CT stimulated the activity of CK2α wild-type but was ineffective on the CK2α K74–77A mutant.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)02781-8</identifier><identifier>PMID: 11557039</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Binding Sites ; Casein Kinase II ; Catalytic Domain ; CK2, protein kinase CK2 (formerly casein kinase 2 or II) ; Grp94 ; Grp94, glucose-regulated protein of 94 kDa (also known as gp96, endoplasmin or hsp100) ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - metabolism ; hsp90, heat shock protein of 90 kDa ; Humans ; Lysine ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Molecular chaperone ; Molecular Sequence Data ; Mutation ; Peptides - metabolism ; Protein kinase CK2 ; Protein Subunits ; Protein-Serine-Threonine Kinases - metabolism ; SPR, surface plasmon resonance ; Substrate Specificity ; Surface Plasmon Resonance ; wt, wild-type</subject><ispartof>FEBS letters, 2001-09, Vol.505 (1), p.42-46</ispartof><rights>2001 Federation of European Biochemical Societies</rights><rights>FEBS Letters 505 (2001) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4268-1792f1bd9985acf08622360adffd470af408ca09c4e2346a6b91a9162868f4b33</citedby><cites>FETCH-LOGICAL-c4268-1792f1bd9985acf08622360adffd470af408ca09c4e2346a6b91a9162868f4b33</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%2FS0014-5793%2801%2902781-8$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(01)02781-8$$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/11557039$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roher, Nerea</creatorcontrib><creatorcontrib>Sarno, Stefania</creatorcontrib><creatorcontrib>Miró, Francesc</creatorcontrib><creatorcontrib>Ruzzene, Maria</creatorcontrib><creatorcontrib>Llorens, Franc</creatorcontrib><creatorcontrib>Meggio, Flavio</creatorcontrib><creatorcontrib>Itarte, Emilio</creatorcontrib><creatorcontrib>Pinna, Lorenzo A</creatorcontrib><creatorcontrib>Plana, Maria</creatorcontrib><title>The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518–803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2α) under non-stressed conditions. A
K
D of 4×10
−7 was determined for this binding. Heparin competed with Grp94-CT for binding to CK2α. CK2β also inhibited the binding of Grp94-CT to CK2α, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2α mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74–77) present in helix C of CK2α. Grp94-CT stimulated the activity of CK2α wild-type but was ineffective on the CK2α K74–77A mutant.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Casein Kinase II</subject><subject>Catalytic Domain</subject><subject>CK2, protein kinase CK2 (formerly casein kinase 2 or II)</subject><subject>Grp94</subject><subject>Grp94, glucose-regulated protein of 94 kDa (also known as gp96, endoplasmin or hsp100)</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>hsp90, heat shock protein of 90 kDa</subject><subject>Humans</subject><subject>Lysine</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular chaperone</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Peptides - metabolism</subject><subject>Protein kinase CK2</subject><subject>Protein Subunits</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>SPR, surface plasmon resonance</subject><subject>Substrate Specificity</subject><subject>Surface Plasmon Resonance</subject><subject>wt, wild-type</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM9u1DAQxq0KRJfCIxT5hMoh1OM4iX1C7ap_EJV6oNyQLMcZq6ZJvNhZYHkrXoRnwtldlSOcLM_3m29mPkKOgb0FBvXpR8ZAFFWjyhMGbxhvJBTygCxANmVRilo-IYtH5JA8T-kLy38J6hk5BKiqhpVqQT7f3SO1Jrbhx6aYMA5-ND3twmD8SIOjV3GlBG392CU6BbqKYcKsPGQsIV1-4L9_0XY90TFMs54L9D70AcefmwFfkKfO9Alf7t8j8uny4m55XdzcXr1fnt0UVvBaFtAo7qDtlJKVsY7JmvOyZqZzrhMNM04waQ1TViDPl5m6VWAU1FzW0om2LI_I651vXu_rGtOkB58s9r0ZMayTbgAakFJksNqBNoaUIjq9in4wcaOB6TlWvY1Vz5lpBnobq5a579V-wLodsPvbtc8xA9c74LvvcfN_rvry4pxvlVlgsC3Ps97trDAn9s1j1Ml6HC12PqKddBf8P7b9AwZAmjQ</recordid><startdate>20010907</startdate><enddate>20010907</enddate><creator>Roher, Nerea</creator><creator>Sarno, Stefania</creator><creator>Miró, Francesc</creator><creator>Ruzzene, Maria</creator><creator>Llorens, Franc</creator><creator>Meggio, Flavio</creator><creator>Itarte, Emilio</creator><creator>Pinna, Lorenzo A</creator><creator>Plana, Maria</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>20010907</creationdate><title>The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme</title><author>Roher, Nerea ; Sarno, Stefania ; Miró, Francesc ; Ruzzene, Maria ; Llorens, Franc ; Meggio, Flavio ; Itarte, Emilio ; Pinna, Lorenzo A ; Plana, Maria</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4268-1792f1bd9985acf08622360adffd470af408ca09c4e2346a6b91a9162868f4b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Casein Kinase II</topic><topic>Catalytic Domain</topic><topic>CK2, protein kinase CK2 (formerly casein kinase 2 or II)</topic><topic>Grp94</topic><topic>Grp94, glucose-regulated protein of 94 kDa (also known as gp96, endoplasmin or hsp100)</topic><topic>HSP70 Heat-Shock Proteins - genetics</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>hsp90, heat shock protein of 90 kDa</topic><topic>Humans</topic><topic>Lysine</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular chaperone</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Peptides - metabolism</topic><topic>Protein kinase CK2</topic><topic>Protein Subunits</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>SPR, surface plasmon resonance</topic><topic>Substrate Specificity</topic><topic>Surface Plasmon Resonance</topic><topic>wt, wild-type</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roher, Nerea</creatorcontrib><creatorcontrib>Sarno, Stefania</creatorcontrib><creatorcontrib>Miró, Francesc</creatorcontrib><creatorcontrib>Ruzzene, Maria</creatorcontrib><creatorcontrib>Llorens, Franc</creatorcontrib><creatorcontrib>Meggio, Flavio</creatorcontrib><creatorcontrib>Itarte, Emilio</creatorcontrib><creatorcontrib>Pinna, Lorenzo A</creatorcontrib><creatorcontrib>Plana, Maria</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>Roher, Nerea</au><au>Sarno, Stefania</au><au>Miró, Francesc</au><au>Ruzzene, Maria</au><au>Llorens, Franc</au><au>Meggio, Flavio</au><au>Itarte, Emilio</au><au>Pinna, Lorenzo A</au><au>Plana, Maria</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-09-07</date><risdate>2001</risdate><volume>505</volume><issue>1</issue><spage>42</spage><epage>46</epage><pages>42-46</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518–803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2α) under non-stressed conditions. A
K
D of 4×10
−7 was determined for this binding. Heparin competed with Grp94-CT for binding to CK2α. CK2β also inhibited the binding of Grp94-CT to CK2α, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2α mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74–77) present in helix C of CK2α. Grp94-CT stimulated the activity of CK2α wild-type but was ineffective on the CK2α K74–77A mutant.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11557039</pmid><doi>10.1016/S0014-5793(01)02781-8</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Free Content; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via Wiley Online Library; Access via ScienceDirect (Elsevier); Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Binding Sites Casein Kinase II Catalytic Domain CK2, protein kinase CK2 (formerly casein kinase 2 or II) Grp94 Grp94, glucose-regulated protein of 94 kDa (also known as gp96, endoplasmin or hsp100) HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism hsp90, heat shock protein of 90 kDa Humans Lysine Membrane Proteins - genetics Membrane Proteins - metabolism Molecular chaperone Molecular Sequence Data Mutation Peptides - metabolism Protein kinase CK2 Protein Subunits Protein-Serine-Threonine Kinases - metabolism SPR, surface plasmon resonance Substrate Specificity Surface Plasmon Resonance wt, wild-type |
| title | The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme |
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