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We began analyzing https://link.springer.com/protocol/10.1007/978-1-61779-430-8_8, but it redirected us to https://link.springer.com/protocol/10.1007/978-1-61779-430-8_8. The analysis below is for the second page.

Title[redir]:
Detection of Cytoplasmic and Nuclear Functions of mTOR by Fractionation | SpringerLink
Description:
Subcellular localization constitutes the environment in which proteins act. It tightly controls access to and availability of different types of molecular interacting partners and is therefore a major determinant of protein function and regulation. Originally thought...

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Keywords {🔍}

article, google, scholar, mtor, pubmed, cas, cell, mammalian, rapamycin, target, mtorc, biol, protein, complex, protocol, chem, localization, rosner, access, mol, privacy, cookies, content, information, publish, cytoplasmic, hengstschläger, kinase, cells, signaling, search, nuclear, fractionation, regulation, sci, translation, nature, usa, download, vienna, springer, usd, essential, function, personal, data, log, journal, research, markus,

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yy1-pgc-1alpha transcriptional complex month download article/chapter cytoplasmic/nuclear protein shuttling tightly controls access conditions privacy policy privacy choices/manage cookies rna polymerase i device instant download iii-transcribed genes pkcalpha-dependent manner humana press journal finder publish ribosomal s6 kinase nutrient-sensitive complex regulating nucleocytoplasmic localiztaion predominant nuclear localization mtor/rictor complex cytoplasmic-nuclear shuttling european economic area long-term treatment proud cg senses osmotic stress mccoy jp jr 5s rrna genes herzfelder’sche familienstiftung editor information editors protocol rosner mere cytoplasmic kinase translation meets transformation molecular interacting partners golgi localization sequences cell growth machinery study protein localization intracellular compartments including protein synthetic machinery cellular signaling symphony essential binding partners mtorc2 components rictor accepting optional cookies author information authors mtor/raptor complex markus hengstschläger rapamycin triggers dephosphorylation protein kinases mtor protein complexes mtorc1 main content log online expanding mtor signalling rapamycin-sensitive signaling mtor-inhibitor rapamycin

Schema {🗺️}

ScholarlyArticle:
      headline:Detection of Cytoplasmic and Nuclear Functions of mTOR by Fractionation
      pageEnd:124
      pageStart:105
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-61779-430-8.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:mTOR
         isbn:
            978-1-61779-430-8
            978-1-61779-429-2
         type:Book
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Margit Rosner
            affiliation:
                  name:Medical University of Vienna
                  address:
                     name:Medical Genetics, Medical University of Vienna, Vienna, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Markus Hengstschläger
            affiliation:
                  name:Medical University of Vienna
                  address:
                     name:Medical Genetics, Medical University of Vienna, Vienna, Austria
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:mTORC1, mTORC2, CHAPS, Fractionation, Cytoplasm, Nucleus, Cytoplasmic-nuclear translocation
      description:Subcellular localization constitutes the environment in which proteins act. It tightly controls access to and availability of different types of molecular interacting partners and is therefore a major determinant of protein function and regulation. Originally thought to be a mere cytoplasmic kinase the mammalian target of rapamycin (mTOR) has recently been localized to various intracellular compartments including the nucleus and specific components of the endomembrane system such as lysosomes. The identification of essential binding partners and the structural and functional partitioning of mTOR into two distinct multiprotein complexes warrant the detailed investigation of the subcellular localization of mTOR as part of mTORC1 and mTORC2. Upon establishment of experimental conditions allowing cytoplasmic/nuclear fractionation at high purity and maximum mTOR complex recovery we have previously shown that the mTOR/raptor complex (mTORC1) is predominantly cytoplasmic whereas the mTOR/rictor complex (mTORC2) is abundant in both compartments. Moreover, the mTORC2 complex components rictor and sin1 are dephosphorylated and dynamically distributed between the cytoplasm and the nucleus upon long-term treatment with the mTOR-inhibitor rapamycin. These findings further demonstrate that the here presented and detailly described fractionation procedure is a valuable tool to study protein localization and cytoplasmic/nuclear protein shuttling in the context of expanding mTOR signalling.
      datePublished:2012
      isAccessibleForFree:
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         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:mTOR
      isbn:
         978-1-61779-430-8
         978-1-61779-429-2
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Medical University of Vienna
      address:
         name:Medical Genetics, Medical University of Vienna, Vienna, Austria
         type:PostalAddress
      name:Medical University of Vienna
      address:
         name:Medical Genetics, Medical University of Vienna, Vienna, Austria
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Margit Rosner
      affiliation:
            name:Medical University of Vienna
            address:
               name:Medical Genetics, Medical University of Vienna, Vienna, Austria
               type:PostalAddress
            type:Organization
      name:Markus Hengstschläger
      affiliation:
            name:Medical University of Vienna
            address:
               name:Medical Genetics, Medical University of Vienna, Vienna, Austria
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Medical Genetics, Medical University of Vienna, Vienna, Austria
      name:Medical Genetics, Medical University of Vienna, Vienna, Austria
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

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