Dissecting subdomains involved in multiple functions of the CK2β subunit
Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical...
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1999 |
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| Umfang: |
8 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Molecular and cellular biochemistry - 1973, 191(1999) vom: Jan./Feb., Seite 43-50 |
| Übergeordnetes Werk: |
volume:191 ; year:1999 ; month:01/02 ; pages:43-50 ; extent:8 |
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| 245 | 1 | 0 | |a Dissecting subdomains involved in multiple functions of the CK2β subunit |
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| 520 | |a Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. | ||
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| 700 | 1 | |a Filhol, Odile |4 oth | |
| 700 | 1 | |a Quintaine, Nora |4 oth | |
| 700 | 1 | |a Sarrouilhe, Denis |4 oth | |
| 700 | 1 | |a Loue-Mackenbach, Petra |4 oth | |
| 700 | 1 | |a Chambaz, Edmond M. |4 oth | |
| 700 | 1 | |a Cochet, Claude |4 oth | |
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(DE-627)NLEJ198049935 DE-627 ger DE-627 rakwb eng Dissecting subdomains involved in multiple functions of the CK2β subunit 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. Springer Online Journal Archives 1860-2002 Leroy, Didier oth Filhol, Odile oth Quintaine, Nora oth Sarrouilhe, Denis oth Loue-Mackenbach, Petra oth Chambaz, Edmond M. oth Cochet, Claude oth in Molecular and cellular biochemistry 1973 191(1999) vom: Jan./Feb., Seite 43-50 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:191 year:1999 month:01/02 pages:43-50 extent:8 http://dx.doi.org/10.1023/A:1006832312169 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 191 1999 1/2 43-50 8 |
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(DE-627)NLEJ198049935 DE-627 ger DE-627 rakwb eng Dissecting subdomains involved in multiple functions of the CK2β subunit 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. Springer Online Journal Archives 1860-2002 Leroy, Didier oth Filhol, Odile oth Quintaine, Nora oth Sarrouilhe, Denis oth Loue-Mackenbach, Petra oth Chambaz, Edmond M. oth Cochet, Claude oth in Molecular and cellular biochemistry 1973 191(1999) vom: Jan./Feb., Seite 43-50 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:191 year:1999 month:01/02 pages:43-50 extent:8 http://dx.doi.org/10.1023/A:1006832312169 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 191 1999 1/2 43-50 8 |
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(DE-627)NLEJ198049935 DE-627 ger DE-627 rakwb eng Dissecting subdomains involved in multiple functions of the CK2β subunit 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. Springer Online Journal Archives 1860-2002 Leroy, Didier oth Filhol, Odile oth Quintaine, Nora oth Sarrouilhe, Denis oth Loue-Mackenbach, Petra oth Chambaz, Edmond M. oth Cochet, Claude oth in Molecular and cellular biochemistry 1973 191(1999) vom: Jan./Feb., Seite 43-50 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:191 year:1999 month:01/02 pages:43-50 extent:8 http://dx.doi.org/10.1023/A:1006832312169 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 191 1999 1/2 43-50 8 |
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(DE-627)NLEJ198049935 DE-627 ger DE-627 rakwb eng Dissecting subdomains involved in multiple functions of the CK2β subunit 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. Springer Online Journal Archives 1860-2002 Leroy, Didier oth Filhol, Odile oth Quintaine, Nora oth Sarrouilhe, Denis oth Loue-Mackenbach, Petra oth Chambaz, Edmond M. oth Cochet, Claude oth in Molecular and cellular biochemistry 1973 191(1999) vom: Jan./Feb., Seite 43-50 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:191 year:1999 month:01/02 pages:43-50 extent:8 http://dx.doi.org/10.1023/A:1006832312169 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 191 1999 1/2 43-50 8 |
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(DE-627)NLEJ198049935 DE-627 ger DE-627 rakwb eng Dissecting subdomains involved in multiple functions of the CK2β subunit 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. Springer Online Journal Archives 1860-2002 Leroy, Didier oth Filhol, Odile oth Quintaine, Nora oth Sarrouilhe, Denis oth Loue-Mackenbach, Petra oth Chambaz, Edmond M. oth Cochet, Claude oth in Molecular and cellular biochemistry 1973 191(1999) vom: Jan./Feb., Seite 43-50 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:191 year:1999 month:01/02 pages:43-50 extent:8 http://dx.doi.org/10.1023/A:1006832312169 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 191 1999 1/2 43-50 8 |
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Leroy, Didier @@oth@@ Filhol, Odile @@oth@@ Quintaine, Nora @@oth@@ Sarrouilhe, Denis @@oth@@ Loue-Mackenbach, Petra @@oth@@ Chambaz, Edmond M. @@oth@@ Cochet, Claude @@oth@@ |
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Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. |
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Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. |
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Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ198049935</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705232037.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070527s1999 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ198049935</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Dissecting subdomains involved in multiple functions of the CK2β subunit</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1999</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">8</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Leroy, Didier</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Filhol, Odile</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Quintaine, Nora</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sarrouilhe, Denis</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Loue-Mackenbach, Petra</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chambaz, Edmond M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cochet, Claude</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Molecular and cellular biochemistry</subfield><subfield code="d">1973</subfield><subfield code="g">191(1999) vom: Jan./Feb., Seite 43-50</subfield><subfield code="w">(DE-627)NLEJ188989099</subfield><subfield code="w">(DE-600)2003615-2</subfield><subfield code="x">1573-4919</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:191</subfield><subfield code="g">year:1999</subfield><subfield code="g">month:01/02</subfield><subfield code="g">pages:43-50</subfield><subfield code="g">extent:8</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1023/A:1006832312169</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">191</subfield><subfield code="j">1999</subfield><subfield code="c">1/2</subfield><subfield code="h">43-50</subfield><subfield code="g">8</subfield></datafield></record></collection>
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7.3997183 |