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Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells.

Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells. Research Abstract Details 

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  • Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells. Abstract Text:

    brent r martinBrent R Martin,thomas j deerinckThomas J Deerinck,mark h ellismanMark H Ellisman,susan s taylorSusan S Taylor,roger y tsienRoger Y Tsien,

    The tetracysteine sequence YRECCPGCCMWR fused to the N terminus of green fluorescent protein (GFP) self-aggregates upon biarsenical labeling in living cells or in vitro. Such dye-triggered aggregates form temperature-dependent morphologies and are dispersed by photobleaching. Fusion of the biarsenical aggregating GFP to the regulatory (R) or catalytic (C) subunit of PKA traps intact holoenzyme in compact fluorescent puncta upon biarsenical labeling. Contrary to the classical model of PKA activation, elevated cAMP does not allow RIalpha and Calpha to diffuse far apart unless the pseudosubstrate inhibitor PKI or locally concentrated substrate is coexpressed. However, RIIalpha releases Calpha upon elevated cAMP alone, dependent on autophosphorylation of the RIIalpha inhibitory domain. DAKAP1alpha overexpression induced R and C outer mitochondrial colocalization and showed similar regulation. Overall, effective separation of type I PKA is substrate dependent, whereas type II PKA dissociation relies on autophosphorylation.

    Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells. Publishing Authors By Initials

    br martinBR Martin,tj deerinckTJ Deerinck,mh ellismanMH Ellisman,ss taylorSS Taylor,ry tsienRY Tsien,

    For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

    PUBMED ID PMID:

    MEDLINE DATE:

    Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Chemistry & biology

    VOLUME: 14

    Page Numbers: 1031-42

    Journal Abbreviation: Chem. Biol.

    ISSN: 1074-5521

    DAY: 30

    MONTH: Sep

    YEAR: 2007

    Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9500160

    Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells. Keywords Mesh Terms:

    KEYWORDS: Temperature

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells. Information

    Substance Name: PRKACA protein, human

    Registry Number: EC 2.7.11.11

    Grant and Affiliation Information for Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells.

    AFFILIATION: Department of Pharmacology, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NCRR

    GRANT: P41 RR004050

    ACRONYM: RR

    MEDLINETA: Chem Biol

    REFSOURCE:

    DATABASENAME:

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