Protein kinase A phosphorylates retinal phosducin on serine 73 in situ
Photoreceptors of vertebrate retinas contain a 33,000-dalton phosphoprotein, phosducin, which complexes with the beta, gamma subunits of the photoreceptor G-protein (guanine nucleotide-binding protein), transducin. In situ, the retinal content of phosphorylated phosducin is modulated by light in con...
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| Veröffentlicht in: | The Journal of biological chemistry 1990-09, Vol.265 (26), p.15860-15866 |
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| description | Photoreceptors of vertebrate retinas contain a 33,000-dalton phosphoprotein, phosducin, which complexes with the beta, gamma
subunits of the photoreceptor G-protein (guanine nucleotide-binding protein), transducin. In situ, the retinal content of
phosphorylated phosducin is modulated by light in conjunction with light-triggered changes in intracellular cyclic nucleotide
concentration. In vitro, phosducin is phosphorylated by either exogenous or endogenous protein kinase A. 32P-Labeled rat retina
phosducin was isolated by immunoprecipitation either after phosphorylation by protein kinase A in the presence of [gamma-32P]ATP
or after incubation of retinas in darkness with 32Pi. In either case, phosphoamino acid analysis showed that greater than
98% of 32P was linked to serine, with less than 2% to threonine. Two-dimensional peptide mapping showed that [32P]phosphoserine
was associated with the same characteristic set of tryptic peptides. Furthermore, Cleveland peptide analysis using four different
proteases showed that either sample exhibited identical patterns of phosphopeptides which were characteristic of the protease
used. Identical phosphopeptide maps were also obtained from 32P-labeled bovine retina phosducin, indicating that the serine
phosphorylation site for protein kinase A is conserved between rat and bovine. Edman degradation of phosphopeptides derived
from 32P-labeled bovine phosducin showed that radioactive phosphate was incorporated into serine residue 73 which is located
within a consensus phosphorylation sequence for protein kinase A (-R-K-M-S73(P)-). These observations are uniformly in agreement
with protein kinase A being the endogenous kinase that phosphorylates phosducin in vivo. |
| doi_str_mv | 10.1016/S0021-9258(18)55478-8 |
| format | Article |
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subunits of the photoreceptor G-protein (guanine nucleotide-binding protein), transducin. In situ, the retinal content of
phosphorylated phosducin is modulated by light in conjunction with light-triggered changes in intracellular cyclic nucleotide
concentration. In vitro, phosducin is phosphorylated by either exogenous or endogenous protein kinase A. 32P-Labeled rat retina
phosducin was isolated by immunoprecipitation either after phosphorylation by protein kinase A in the presence of [gamma-32P]ATP
or after incubation of retinas in darkness with 32Pi. In either case, phosphoamino acid analysis showed that greater than
98% of 32P was linked to serine, with less than 2% to threonine. Two-dimensional peptide mapping showed that [32P]phosphoserine
was associated with the same characteristic set of tryptic peptides. Furthermore, Cleveland peptide analysis using four different
proteases showed that either sample exhibited identical patterns of phosphopeptides which were characteristic of the protease
used. Identical phosphopeptide maps were also obtained from 32P-labeled bovine retina phosducin, indicating that the serine
phosphorylation site for protein kinase A is conserved between rat and bovine. Edman degradation of phosphopeptides derived
from 32P-labeled bovine phosducin showed that radioactive phosphate was incorporated into serine residue 73 which is located
within a consensus phosphorylation sequence for protein kinase A (-R-K-M-S73(P)-). These observations are uniformly in agreement
with protein kinase A being the endogenous kinase that phosphorylates phosducin in vivo.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)55478-8</identifier><identifier>PMID: 2394752</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>550201 - Biochemistry- Tracer Techniques ; Adenosine Triphosphate - metabolism ; AMINO ACID SEQUENCE ; ANIMALS ; ANTIBODIES ; Antibodies, Monoclonal ; ATP ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BETA-MINUS DECAY RADIOISOTOPES ; BIOASSAY ; BIOCHEMICAL REACTION KINETICS ; Blotting, Western ; BODY ; BODY AREAS ; CATTAILS ; CATTLE ; CHEMICAL REACTIONS ; CHROMATOGRAPHY ; Chromatography, High Pressure Liquid ; Cyanogen Bromide ; DAYS LIVING RADIOISOTOPES ; DOMESTIC ANIMALS ; ENZYME ACTIVITY ; ENZYMES ; Eye Proteins - isolation & purification ; Eye Proteins - metabolism ; EYES ; FACE ; GTP-Binding Protein Regulators ; HEAD ; IMMUNOASSAY ; ISOTOPE APPLICATIONS ; ISOTOPES ; KINETICS ; LIGHT NUCLEI ; LILIOPSIDA ; LIQUID COLUMN CHROMATOGRAPHY ; MAGNOLIOPHYTA ; MAMMALS ; Molecular Sequence Data ; MOLECULAR STRUCTURE ; MONOCLONAL ANTIBODIES ; NUCLEI ; NUCLEOTIDES ; ODD-ODD NUCLEI ; ORGANIC COMPOUNDS ; ORGANS ; Peptide Fragments - isolation & purification ; PEPTIDES ; phosducin ; Phosphopeptides - isolation & purification ; Phosphoproteins - isolation & purification ; Phosphoproteins - metabolism ; PHOSPHORUS 32 ; PHOSPHORUS ISOTOPES ; Phosphorus Radioisotopes ; PHOSPHORUS-GROUP TRANSFERASES ; PHOSPHORYLATION ; PHOSPHOTRANSFERASES ; PLANTS ; Protein Kinases - metabolism ; PROTEINS ; RADIOISOTOPES ; RATS ; Rats, Inbred Strains ; REACTION KINETICS ; RETINA ; Retina - metabolism ; RODENTS ; RUMINANTS ; SENSE ORGANS ; SEPARATION PROCESSES ; Substrate Specificity ; TRACER TECHNIQUES ; TRANSFERASES ; VERTEBRATES</subject><ispartof>The Journal of biological chemistry, 1990-09, Vol.265 (26), p.15860-15866</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3538-4450191f97f5b7e832eb269fa1f48088c8fc6e291f33b622d3db9af697e4a6273</citedby><cites>FETCH-LOGICAL-c3538-4450191f97f5b7e832eb269fa1f48088c8fc6e291f33b622d3db9af697e4a6273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2394752$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6374365$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, R H</creatorcontrib><creatorcontrib>Brown, B M</creatorcontrib><creatorcontrib>Lolley, R N</creatorcontrib><title>Protein kinase A phosphorylates retinal phosducin on serine 73 in situ</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Photoreceptors of vertebrate retinas contain a 33,000-dalton phosphoprotein, phosducin, which complexes with the beta, gamma
subunits of the photoreceptor G-protein (guanine nucleotide-binding protein), transducin. In situ, the retinal content of
phosphorylated phosducin is modulated by light in conjunction with light-triggered changes in intracellular cyclic nucleotide
concentration. In vitro, phosducin is phosphorylated by either exogenous or endogenous protein kinase A. 32P-Labeled rat retina
phosducin was isolated by immunoprecipitation either after phosphorylation by protein kinase A in the presence of [gamma-32P]ATP
or after incubation of retinas in darkness with 32Pi. In either case, phosphoamino acid analysis showed that greater than
98% of 32P was linked to serine, with less than 2% to threonine. Two-dimensional peptide mapping showed that [32P]phosphoserine
was associated with the same characteristic set of tryptic peptides. Furthermore, Cleveland peptide analysis using four different
proteases showed that either sample exhibited identical patterns of phosphopeptides which were characteristic of the protease
used. Identical phosphopeptide maps were also obtained from 32P-labeled bovine retina phosducin, indicating that the serine
phosphorylation site for protein kinase A is conserved between rat and bovine. Edman degradation of phosphopeptides derived
from 32P-labeled bovine phosducin showed that radioactive phosphate was incorporated into serine residue 73 which is located
within a consensus phosphorylation sequence for protein kinase A (-R-K-M-S73(P)-). These observations are uniformly in agreement
with protein kinase A being the endogenous kinase that phosphorylates phosducin in vivo.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>AMINO ACID SEQUENCE</subject><subject>ANIMALS</subject><subject>ANTIBODIES</subject><subject>Antibodies, Monoclonal</subject><subject>ATP</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>BIOASSAY</subject><subject>BIOCHEMICAL REACTION KINETICS</subject><subject>Blotting, Western</subject><subject>BODY</subject><subject>BODY AREAS</subject><subject>CATTAILS</subject><subject>CATTLE</subject><subject>CHEMICAL REACTIONS</subject><subject>CHROMATOGRAPHY</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cyanogen Bromide</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DOMESTIC ANIMALS</subject><subject>ENZYME ACTIVITY</subject><subject>ENZYMES</subject><subject>Eye Proteins - isolation & purification</subject><subject>Eye Proteins - metabolism</subject><subject>EYES</subject><subject>FACE</subject><subject>GTP-Binding Protein Regulators</subject><subject>HEAD</subject><subject>IMMUNOASSAY</subject><subject>ISOTOPE APPLICATIONS</subject><subject>ISOTOPES</subject><subject>KINETICS</subject><subject>LIGHT NUCLEI</subject><subject>LILIOPSIDA</subject><subject>LIQUID COLUMN CHROMATOGRAPHY</subject><subject>MAGNOLIOPHYTA</subject><subject>MAMMALS</subject><subject>Molecular Sequence Data</subject><subject>MOLECULAR STRUCTURE</subject><subject>MONOCLONAL ANTIBODIES</subject><subject>NUCLEI</subject><subject>NUCLEOTIDES</subject><subject>ODD-ODD NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANS</subject><subject>Peptide Fragments - isolation & purification</subject><subject>PEPTIDES</subject><subject>phosducin</subject><subject>Phosphopeptides - isolation & purification</subject><subject>Phosphoproteins - isolation & purification</subject><subject>Phosphoproteins - metabolism</subject><subject>PHOSPHORUS 32</subject><subject>PHOSPHORUS ISOTOPES</subject><subject>Phosphorus Radioisotopes</subject><subject>PHOSPHORUS-GROUP TRANSFERASES</subject><subject>PHOSPHORYLATION</subject><subject>PHOSPHOTRANSFERASES</subject><subject>PLANTS</subject><subject>Protein Kinases - metabolism</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>RATS</subject><subject>Rats, Inbred Strains</subject><subject>REACTION KINETICS</subject><subject>RETINA</subject><subject>Retina - metabolism</subject><subject>RODENTS</subject><subject>RUMINANTS</subject><subject>SENSE ORGANS</subject><subject>SEPARATION PROCESSES</subject><subject>Substrate Specificity</subject><subject>TRACER TECHNIQUES</subject><subject>TRANSFERASES</subject><subject>VERTEBRATES</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdlKxTAQhoMoelweQSgiohfV7MuliBsICip4F9qcqY32NMekRXx7cxa8NTCEzP9NZpgfoUOCzwkm8uIZY0pKQ4U-JfpMCK50qTfQhGDNSibI2yaa_CE7aDelD5wPN2QbbVNmuBJ0gm6eYhjA98Wn76sExWUxb0PKEX-6aoBURBiy0i3T09FlMvRFguh7KBQr8jv5YdxHW03VJThY33vo9eb65equfHi8vb-6fCgdE0yXnAtMDGmMakStQDMKNZWmqUjDNdba6cZJoJlgrJaUTtm0NlUjjQJeSarYHjpa_RvS4G1yfgDXutD34AYrmeJMigydrKB5DF8jpMHOfHLQdVUPYUxWGaOxFPpfkAilCNcmg2IFuhhSitDYefSzKv5Ygu3CDbt0wy5WbYm2SzfsosHhusFYz2D6V7Vef9aPV3rr39tvH8HWPrgWZpZKkSNPoCVmv-7Jj2w</recordid><startdate>19900915</startdate><enddate>19900915</enddate><creator>Lee, R H</creator><creator>Brown, B M</creator><creator>Lolley, R N</creator><general>American Society for Biochemistry and Molecular Biology</general><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19900915</creationdate><title>Protein kinase A phosphorylates retinal phosducin on serine 73 in situ</title><author>Lee, R H ; Brown, B M ; Lolley, R N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3538-4450191f97f5b7e832eb269fa1f48088c8fc6e291f33b622d3db9af697e4a6273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>AMINO ACID SEQUENCE</topic><topic>ANIMALS</topic><topic>ANTIBODIES</topic><topic>Antibodies, Monoclonal</topic><topic>ATP</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>BIOASSAY</topic><topic>BIOCHEMICAL REACTION KINETICS</topic><topic>Blotting, Western</topic><topic>BODY</topic><topic>BODY AREAS</topic><topic>CATTAILS</topic><topic>CATTLE</topic><topic>CHEMICAL REACTIONS</topic><topic>CHROMATOGRAPHY</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cyanogen Bromide</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DOMESTIC ANIMALS</topic><topic>ENZYME ACTIVITY</topic><topic>ENZYMES</topic><topic>Eye Proteins - isolation & purification</topic><topic>Eye Proteins - metabolism</topic><topic>EYES</topic><topic>FACE</topic><topic>GTP-Binding Protein Regulators</topic><topic>HEAD</topic><topic>IMMUNOASSAY</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPES</topic><topic>KINETICS</topic><topic>LIGHT NUCLEI</topic><topic>LILIOPSIDA</topic><topic>LIQUID COLUMN CHROMATOGRAPHY</topic><topic>MAGNOLIOPHYTA</topic><topic>MAMMALS</topic><topic>Molecular Sequence Data</topic><topic>MOLECULAR STRUCTURE</topic><topic>MONOCLONAL ANTIBODIES</topic><topic>NUCLEI</topic><topic>NUCLEOTIDES</topic><topic>ODD-ODD NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANS</topic><topic>Peptide Fragments - isolation & purification</topic><topic>PEPTIDES</topic><topic>phosducin</topic><topic>Phosphopeptides - isolation & purification</topic><topic>Phosphoproteins - isolation & purification</topic><topic>Phosphoproteins - metabolism</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>Phosphorus Radioisotopes</topic><topic>PHOSPHORUS-GROUP TRANSFERASES</topic><topic>PHOSPHORYLATION</topic><topic>PHOSPHOTRANSFERASES</topic><topic>PLANTS</topic><topic>Protein Kinases - metabolism</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>RATS</topic><topic>Rats, Inbred Strains</topic><topic>REACTION KINETICS</topic><topic>RETINA</topic><topic>Retina - metabolism</topic><topic>RODENTS</topic><topic>RUMINANTS</topic><topic>SENSE ORGANS</topic><topic>SEPARATION PROCESSES</topic><topic>Substrate Specificity</topic><topic>TRACER TECHNIQUES</topic><topic>TRANSFERASES</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, R H</creatorcontrib><creatorcontrib>Brown, B M</creatorcontrib><creatorcontrib>Lolley, R N</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, R H</au><au>Brown, B M</au><au>Lolley, R N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein kinase A phosphorylates retinal phosducin on serine 73 in situ</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-09-15</date><risdate>1990</risdate><volume>265</volume><issue>26</issue><spage>15860</spage><epage>15866</epage><pages>15860-15866</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Photoreceptors of vertebrate retinas contain a 33,000-dalton phosphoprotein, phosducin, which complexes with the beta, gamma
subunits of the photoreceptor G-protein (guanine nucleotide-binding protein), transducin. In situ, the retinal content of
phosphorylated phosducin is modulated by light in conjunction with light-triggered changes in intracellular cyclic nucleotide
concentration. In vitro, phosducin is phosphorylated by either exogenous or endogenous protein kinase A. 32P-Labeled rat retina
phosducin was isolated by immunoprecipitation either after phosphorylation by protein kinase A in the presence of [gamma-32P]ATP
or after incubation of retinas in darkness with 32Pi. In either case, phosphoamino acid analysis showed that greater than
98% of 32P was linked to serine, with less than 2% to threonine. Two-dimensional peptide mapping showed that [32P]phosphoserine
was associated with the same characteristic set of tryptic peptides. Furthermore, Cleveland peptide analysis using four different
proteases showed that either sample exhibited identical patterns of phosphopeptides which were characteristic of the protease
used. Identical phosphopeptide maps were also obtained from 32P-labeled bovine retina phosducin, indicating that the serine
phosphorylation site for protein kinase A is conserved between rat and bovine. Edman degradation of phosphopeptides derived
from 32P-labeled bovine phosducin showed that radioactive phosphate was incorporated into serine residue 73 which is located
within a consensus phosphorylation sequence for protein kinase A (-R-K-M-S73(P)-). These observations are uniformly in agreement
with protein kinase A being the endogenous kinase that phosphorylates phosducin in vivo.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2394752</pmid><doi>10.1016/S0021-9258(18)55478-8</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1990-09, Vol.265 (26), p.15860-15866 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_osti_scitechconnect_6374365 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 550201 - Biochemistry- Tracer Techniques Adenosine Triphosphate - metabolism AMINO ACID SEQUENCE ANIMALS ANTIBODIES Antibodies, Monoclonal ATP BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES BIOASSAY BIOCHEMICAL REACTION KINETICS Blotting, Western BODY BODY AREAS CATTAILS CATTLE CHEMICAL REACTIONS CHROMATOGRAPHY Chromatography, High Pressure Liquid Cyanogen Bromide DAYS LIVING RADIOISOTOPES DOMESTIC ANIMALS ENZYME ACTIVITY ENZYMES Eye Proteins - isolation & purification Eye Proteins - metabolism EYES FACE GTP-Binding Protein Regulators HEAD IMMUNOASSAY ISOTOPE APPLICATIONS ISOTOPES KINETICS LIGHT NUCLEI LILIOPSIDA LIQUID COLUMN CHROMATOGRAPHY MAGNOLIOPHYTA MAMMALS Molecular Sequence Data MOLECULAR STRUCTURE MONOCLONAL ANTIBODIES NUCLEI NUCLEOTIDES ODD-ODD NUCLEI ORGANIC COMPOUNDS ORGANS Peptide Fragments - isolation & purification PEPTIDES phosducin Phosphopeptides - isolation & purification Phosphoproteins - isolation & purification Phosphoproteins - metabolism PHOSPHORUS 32 PHOSPHORUS ISOTOPES Phosphorus Radioisotopes PHOSPHORUS-GROUP TRANSFERASES PHOSPHORYLATION PHOSPHOTRANSFERASES PLANTS Protein Kinases - metabolism PROTEINS RADIOISOTOPES RATS Rats, Inbred Strains REACTION KINETICS RETINA Retina - metabolism RODENTS RUMINANTS SENSE ORGANS SEPARATION PROCESSES Substrate Specificity TRACER TECHNIQUES TRANSFERASES VERTEBRATES |
| title | Protein kinase A phosphorylates retinal phosducin on serine 73 in situ |
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