Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK
Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activa...
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| Veröffentlicht in: | Biochemical journal 2001-04, Vol.355 (Pt 2), p.297-305 |
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| creator | Lefebvre, D L Bai, Y Shahmolky, N Sharma, M Poon, R Drucker, D J Rosen, C F |
| description | Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76 kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80 kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress. |
| doi_str_mv | 10.1042/0264-6021:3550297 |
| format | Article |
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Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76 kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80 kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/0264-6021:3550297</identifier><identifier>PMID: 11284715</identifier><language>eng</language><publisher>England</publisher><subject>Adenosine Monophosphate - pharmacology ; Amino Acid Sequence ; Aminoimidazole Carboxamide - analogs & derivatives ; Aminoimidazole Carboxamide - pharmacology ; Animals ; Base Sequence ; Cells, Cultured ; Chromosome Mapping ; Cricetinae ; DNA, Complementary ; Enzyme Activation ; Glucose - metabolism ; Humans ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Phosphorylation ; Precipitin Tests ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Rats ; Ribonucleotides - pharmacology ; RNA, Messenger - genetics ; Sequence Homology, Amino Acid ; Substrate Specificity</subject><ispartof>Biochemical journal, 2001-04, Vol.355 (Pt 2), p.297-305</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-43322d818868f40a620fd9ac83e67f3fdfd66bf4f3a99b80e8e85132ac69c0d13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221739/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221739/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11284715$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lefebvre, D L</creatorcontrib><creatorcontrib>Bai, Y</creatorcontrib><creatorcontrib>Shahmolky, N</creatorcontrib><creatorcontrib>Sharma, M</creatorcontrib><creatorcontrib>Poon, R</creatorcontrib><creatorcontrib>Drucker, D J</creatorcontrib><creatorcontrib>Rosen, C F</creatorcontrib><title>Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76 kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80 kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.</description><subject>Adenosine Monophosphate - pharmacology</subject><subject>Amino Acid Sequence</subject><subject>Aminoimidazole Carboxamide - analogs & derivatives</subject><subject>Aminoimidazole Carboxamide - pharmacology</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cells, Cultured</subject><subject>Chromosome Mapping</subject><subject>Cricetinae</subject><subject>DNA, Complementary</subject><subject>Enzyme Activation</subject><subject>Glucose - metabolism</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Molecular Sequence Data</subject><subject>Phosphorylation</subject><subject>Precipitin Tests</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Rats</subject><subject>Ribonucleotides - pharmacology</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkctuFDEQRa0IlAyBD2CDesUKE7_adrNAGkWQRCQB8VhbHrucmPTYE7tnJPIT-WW6NaMQECtLdeteV9VB6CUlbykR7IgwKbAkjL7jbUtYp_bQjApFsFZMP0GzB_0APav1JyFUEEH20QGlTAtF2xm6P_OQhhiis0PMqbHJN-7aFusGKPFuW8yhsU3KG-ibunYlV8ApJxygLCdzumpWJQ8QU3MTk61wNL_4gseEuLED-H9EXKD_T_lN8-1y_vXTc_Q02L7Ci917iH58_PD9-BSffz45O56fYyckHbDgnDGvqdZSB0GsZCT4zjrNQarAgw9eykUQgduuW2gCGnRLObNOdo54yg_R-23uar1YgnfjHsX2ZlXi0pZfJtto_lZSvDZXeWMoY1Txbgx4vQso-XYNdTDLWB30vU2Q19UoNV5ft2pspNvG6XC1QHj4hBIzYTQTJjNhMjuMo-fV4-n-OHbc-G_YQJw6</recordid><startdate>20010415</startdate><enddate>20010415</enddate><creator>Lefebvre, D L</creator><creator>Bai, Y</creator><creator>Shahmolky, N</creator><creator>Sharma, M</creator><creator>Poon, R</creator><creator>Drucker, D J</creator><creator>Rosen, C F</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><scope>5PM</scope></search><sort><creationdate>20010415</creationdate><title>Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK</title><author>Lefebvre, D L ; Bai, Y ; Shahmolky, N ; Sharma, M ; Poon, R ; Drucker, D J ; Rosen, C F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-43322d818868f40a620fd9ac83e67f3fdfd66bf4f3a99b80e8e85132ac69c0d13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Adenosine Monophosphate - pharmacology</topic><topic>Amino Acid Sequence</topic><topic>Aminoimidazole Carboxamide - analogs & derivatives</topic><topic>Aminoimidazole Carboxamide - pharmacology</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cells, Cultured</topic><topic>Chromosome Mapping</topic><topic>Cricetinae</topic><topic>DNA, Complementary</topic><topic>Enzyme Activation</topic><topic>Glucose - metabolism</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Molecular Sequence Data</topic><topic>Phosphorylation</topic><topic>Precipitin Tests</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Rats</topic><topic>Ribonucleotides - pharmacology</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lefebvre, D L</creatorcontrib><creatorcontrib>Bai, Y</creatorcontrib><creatorcontrib>Shahmolky, N</creatorcontrib><creatorcontrib>Sharma, M</creatorcontrib><creatorcontrib>Poon, R</creatorcontrib><creatorcontrib>Drucker, D J</creatorcontrib><creatorcontrib>Rosen, C F</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lefebvre, D L</au><au>Bai, Y</au><au>Shahmolky, N</au><au>Sharma, M</au><au>Poon, R</au><au>Drucker, D J</au><au>Rosen, C F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2001-04-15</date><risdate>2001</risdate><volume>355</volume><issue>Pt 2</issue><spage>297</spage><epage>305</epage><pages>297-305</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76 kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80 kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.</abstract><cop>England</cop><pmid>11284715</pmid><doi>10.1042/0264-6021:3550297</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Monophosphate - pharmacology Amino Acid Sequence Aminoimidazole Carboxamide - analogs & derivatives Aminoimidazole Carboxamide - pharmacology Animals Base Sequence Cells, Cultured Chromosome Mapping Cricetinae DNA, Complementary Enzyme Activation Glucose - metabolism Humans Hydrogen-Ion Concentration Molecular Sequence Data Phosphorylation Precipitin Tests Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Rats Ribonucleotides - pharmacology RNA, Messenger - genetics Sequence Homology, Amino Acid Substrate Specificity |
| title | Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK |
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