Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue.
Identifieur interne : 001B18 ( Main/Exploration ); précédent : 001B17; suivant : 001B19Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue.
Auteurs : J. Chen [États-Unis] ; X F Zheng ; E J Brown ; S L SchreiberSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1995.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Biosynthèse des protéines (MeSH), Cinétique (MeSH), Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Dichroïsme circulaire (MeSH), Données de séquences moléculaires (MeSH), Fragments peptidiques (composition chimique), Fragments peptidiques (métabolisme), Humains (MeSH), Immunosuppresseurs (métabolisme), Mammifères (MeSH), Masse moléculaire (MeSH), Mutagenèse dirigée (MeSH), Polyènes (métabolisme), Protéines de fusion recombinantes (biosynthèse), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (métabolisme), Protéines de liaison au tacrolimus (MeSH), Protéines de liaison à l'ADN (biosynthèse), Protéines de liaison à l'ADN (composition chimique), Protéines de liaison à l'ADN (métabolisme), Protéines de transport (biosynthèse), Protéines de transport (composition chimique), Protéines de transport (métabolisme), Protéines du choc thermique (biosynthèse), Protéines du choc thermique (composition chimique), Protéines du choc thermique (métabolisme), Rats (MeSH), Saccharomyces cerevisiae (métabolisme), Sirolimus (MeSH), Sites de fixation (MeSH), Séquence d'acides aminés (MeSH), Sérine (MeSH), Tacrolimus (métabolisme), Transcription génétique (MeSH).
- MESH :
- biosynthèse : Protéines de fusion recombinantes, Protéines de liaison à l'ADN, Protéines de transport, Protéines du choc thermique.
- composition chimique : Fragments peptidiques, Protéines de fusion recombinantes, Protéines de liaison à l'ADN, Protéines de transport, Protéines du choc thermique.
- métabolisme : Fragments peptidiques, Immunosuppresseurs, Polyènes, Protéines de fusion recombinantes, Protéines de liaison à l'ADN, Protéines de transport, Protéines du choc thermique, Saccharomyces cerevisiae, Tacrolimus.
- Animaux, Biosynthèse des protéines, Cinétique, Clonage moléculaire, Conformation des protéines, Dichroïsme circulaire, Données de séquences moléculaires, Humains, Mammifères, Masse moléculaire, Mutagenèse dirigée, Protéines de liaison au tacrolimus, Rats, Sirolimus, Sites de fixation, Séquence d'acides aminés, Sérine, Transcription génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Binding Sites (MeSH), Carrier Proteins (biosynthesis), Carrier Proteins (chemistry), Carrier Proteins (metabolism), Circular Dichroism (MeSH), Cloning, Molecular (MeSH), DNA-Binding Proteins (biosynthesis), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (metabolism), Heat-Shock Proteins (biosynthesis), Heat-Shock Proteins (chemistry), Heat-Shock Proteins (metabolism), Humans (MeSH), Immunosuppressive Agents (metabolism), Kinetics (MeSH), Mammals (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Mutagenesis, Site-Directed (MeSH), Peptide Fragments (chemistry), Peptide Fragments (metabolism), Polyenes (metabolism), Protein Biosynthesis (MeSH), Protein Conformation (MeSH), Rats (MeSH), Recombinant Fusion Proteins (biosynthesis), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (metabolism), Saccharomyces cerevisiae (metabolism), Serine (MeSH), Sirolimus (MeSH), Tacrolimus (metabolism), Tacrolimus Binding Proteins (MeSH), Transcription, Genetic (MeSH).
- MESH :
- chemical , biosynthesis : Carrier Proteins, DNA-Binding Proteins, Heat-Shock Proteins, Recombinant Fusion Proteins.
- chemical , chemistry : Carrier Proteins, DNA-Binding Proteins, Heat-Shock Proteins, Peptide Fragments, Recombinant Fusion Proteins.
- chemical , metabolism : Carrier Proteins, DNA-Binding Proteins, Heat-Shock Proteins, Immunosuppressive Agents, Peptide Fragments, Polyenes, Recombinant Fusion Proteins, Tacrolimus.
- metabolism : Saccharomyces cerevisiae.
- Amino Acid Sequence, Animals, Binding Sites, Circular Dichroism, Cloning, Molecular, Humans, Kinetics, Mammals, Molecular Sequence Data, Molecular Weight, Mutagenesis, Site-Directed, Protein Biosynthesis, Protein Conformation, Rats, Serine, Sirolimus, Tacrolimus Binding Proteins, Transcription, Genetic.
Abstract
Complexed with its intracellular receptor, FKBP12, the natural product rapamycin inhibits G1 progression of the cell cycle in a variety of mammalian cell lines and in the yeast Saccharomyces cerevisae. Previously, a mammalian protein that directly associates with FKBP12-rapamycin has been identified and its encoding gene has been cloned from both human (designated FRAP) [Brown, E.J., Albers, M.W., Shin, T.B., Ichikawa, K., Keith, C.T., Lane, W.S. & Schreiber, S.L. (1994) Nature (London) 369, 756-758] and rat (designated RAFT) [Sabatini, D.M., Erdjument-Bromage, H., Lui, M., Tempst, P. & Snyder, S.H. (1994) Cell 78, 35-43]. The full-length FRAP is a 289-kDa protein containing a putative phosphatidylinositol kinase domain. Using an in vitro transcription/translation assay method coupled with proteolysis studies, we have identified an 11-kDa FKBP12-rapamycin-binding domain within FRAP. This minimal binding domain lies N-terminal to the kinase domain and spans residues 2025-2114. In addition, we have carried out mutagenesis studies to investigate the role of Ser2035, a potential phosphorylation site for protein kinase C within this domain. We now show that the FRAP Ser2035-->Ala mutant displays similar binding affinity when compared with the wild-type protein, whereas all other mutations at this site, including mimics of phosphoserine, abolish binding, presumably due to either unfavorable steric interactions or induced conformational changes.
DOI: 10.1073/pnas.92.11.4947
PubMed: 7539137
PubMed Central: PMC41824
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue.</title>
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<term>Animals (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Carrier Proteins (biosynthesis)</term>
<term>Carrier Proteins (chemistry)</term>
<term>Carrier Proteins (metabolism)</term>
<term>Circular Dichroism (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>DNA-Binding Proteins (biosynthesis)</term>
<term>DNA-Binding Proteins (chemistry)</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>Heat-Shock Proteins (biosynthesis)</term>
<term>Heat-Shock Proteins (chemistry)</term>
<term>Heat-Shock Proteins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Immunosuppressive Agents (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Mammals (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (metabolism)</term>
<term>Polyenes (metabolism)</term>
<term>Protein Biosynthesis (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Rats (MeSH)</term>
<term>Recombinant Fusion Proteins (biosynthesis)</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Serine (MeSH)</term>
<term>Sirolimus (MeSH)</term>
<term>Tacrolimus (metabolism)</term>
<term>Tacrolimus Binding Proteins (MeSH)</term>
<term>Transcription, Genetic (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Biosynthèse des protéines (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Dichroïsme circulaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Fragments peptidiques (composition chimique)</term>
<term>Fragments peptidiques (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Immunosuppresseurs (métabolisme)</term>
<term>Mammifères (MeSH)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Polyènes (métabolisme)</term>
<term>Protéines de fusion recombinantes (biosynthèse)</term>
<term>Protéines de fusion recombinantes (composition chimique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines de liaison au tacrolimus (MeSH)</term>
<term>Protéines de liaison à l'ADN (biosynthèse)</term>
<term>Protéines de liaison à l'ADN (composition chimique)</term>
<term>Protéines de liaison à l'ADN (métabolisme)</term>
<term>Protéines de transport (biosynthèse)</term>
<term>Protéines de transport (composition chimique)</term>
<term>Protéines de transport (métabolisme)</term>
<term>Protéines du choc thermique (biosynthèse)</term>
<term>Protéines du choc thermique (composition chimique)</term>
<term>Protéines du choc thermique (métabolisme)</term>
<term>Rats (MeSH)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sirolimus (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Sérine (MeSH)</term>
<term>Tacrolimus (métabolisme)</term>
<term>Transcription génétique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Carrier Proteins</term>
<term>DNA-Binding Proteins</term>
<term>Heat-Shock Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carrier Proteins</term>
<term>DNA-Binding Proteins</term>
<term>Heat-Shock Proteins</term>
<term>Peptide Fragments</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term>
<term>DNA-Binding Proteins</term>
<term>Heat-Shock Proteins</term>
<term>Immunosuppressive Agents</term>
<term>Peptide Fragments</term>
<term>Polyenes</term>
<term>Recombinant Fusion Proteins</term>
<term>Tacrolimus</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines de fusion recombinantes</term>
<term>Protéines de liaison à l'ADN</term>
<term>Protéines de transport</term>
<term>Protéines du choc thermique</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Fragments peptidiques</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de liaison à l'ADN</term>
<term>Protéines de transport</term>
<term>Protéines du choc thermique</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fragments peptidiques</term>
<term>Immunosuppresseurs</term>
<term>Polyènes</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de liaison à l'ADN</term>
<term>Protéines de transport</term>
<term>Protéines du choc thermique</term>
<term>Saccharomyces cerevisiae</term>
<term>Tacrolimus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Binding Sites</term>
<term>Circular Dichroism</term>
<term>Cloning, Molecular</term>
<term>Humans</term>
<term>Kinetics</term>
<term>Mammals</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
<term>Mutagenesis, Site-Directed</term>
<term>Protein Biosynthesis</term>
<term>Protein Conformation</term>
<term>Rats</term>
<term>Serine</term>
<term>Sirolimus</term>
<term>Tacrolimus Binding Proteins</term>
<term>Transcription, Genetic</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Biosynthèse des protéines</term>
<term>Cinétique</term>
<term>Clonage moléculaire</term>
<term>Conformation des protéines</term>
<term>Dichroïsme circulaire</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Mammifères</term>
<term>Masse moléculaire</term>
<term>Mutagenèse dirigée</term>
<term>Protéines de liaison au tacrolimus</term>
<term>Rats</term>
<term>Sirolimus</term>
<term>Sites de fixation</term>
<term>Séquence d'acides aminés</term>
<term>Sérine</term>
<term>Transcription génétique</term>
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<front><div type="abstract" xml:lang="en">Complexed with its intracellular receptor, FKBP12, the natural product rapamycin inhibits G1 progression of the cell cycle in a variety of mammalian cell lines and in the yeast Saccharomyces cerevisae. Previously, a mammalian protein that directly associates with FKBP12-rapamycin has been identified and its encoding gene has been cloned from both human (designated FRAP) [Brown, E.J., Albers, M.W., Shin, T.B., Ichikawa, K., Keith, C.T., Lane, W.S. & Schreiber, S.L. (1994) Nature (London) 369, 756-758] and rat (designated RAFT) [Sabatini, D.M., Erdjument-Bromage, H., Lui, M., Tempst, P. & Snyder, S.H. (1994) Cell 78, 35-43]. The full-length FRAP is a 289-kDa protein containing a putative phosphatidylinositol kinase domain. Using an in vitro transcription/translation assay method coupled with proteolysis studies, we have identified an 11-kDa FKBP12-rapamycin-binding domain within FRAP. This minimal binding domain lies N-terminal to the kinase domain and spans residues 2025-2114. In addition, we have carried out mutagenesis studies to investigate the role of Ser2035, a potential phosphorylation site for protein kinase C within this domain. We now show that the FRAP Ser2035-->Ala mutant displays similar binding affinity when compared with the wild-type protein, whereas all other mutations at this site, including mimics of phosphoserine, abolish binding, presumably due to either unfavorable steric interactions or induced conformational changes.</div>
</front>
</TEI>
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<DateCompleted><Year>1995</Year>
<Month>06</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>05</Month>
<Day>01</Day>
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<Article PubModel="Print"><Journal><ISSN IssnType="Print">0027-8424</ISSN>
<JournalIssue CitedMedium="Print"><Volume>92</Volume>
<Issue>11</Issue>
<PubDate><Year>1995</Year>
<Month>May</Month>
<Day>23</Day>
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<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation>
</Journal>
<ArticleTitle>Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue.</ArticleTitle>
<Pagination><MedlinePgn>4947-51</MedlinePgn>
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<Abstract><AbstractText>Complexed with its intracellular receptor, FKBP12, the natural product rapamycin inhibits G1 progression of the cell cycle in a variety of mammalian cell lines and in the yeast Saccharomyces cerevisae. Previously, a mammalian protein that directly associates with FKBP12-rapamycin has been identified and its encoding gene has been cloned from both human (designated FRAP) [Brown, E.J., Albers, M.W., Shin, T.B., Ichikawa, K., Keith, C.T., Lane, W.S. & Schreiber, S.L. (1994) Nature (London) 369, 756-758] and rat (designated RAFT) [Sabatini, D.M., Erdjument-Bromage, H., Lui, M., Tempst, P. & Snyder, S.H. (1994) Cell 78, 35-43]. The full-length FRAP is a 289-kDa protein containing a putative phosphatidylinositol kinase domain. Using an in vitro transcription/translation assay method coupled with proteolysis studies, we have identified an 11-kDa FKBP12-rapamycin-binding domain within FRAP. This minimal binding domain lies N-terminal to the kinase domain and spans residues 2025-2114. In addition, we have carried out mutagenesis studies to investigate the role of Ser2035, a potential phosphorylation site for protein kinase C within this domain. We now show that the FRAP Ser2035-->Ala mutant displays similar binding affinity when compared with the wild-type protein, whereas all other mutations at this site, including mimics of phosphoserine, abolish binding, presumably due to either unfavorable steric interactions or induced conformational changes.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
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<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
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<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
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