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  1. Article ; Online: Pseudoscaffolds and anchoring proteins: the difference is in the details.

    Aggarwal-Howarth, Stacey / Scott, John D

    Biochemical Society transactions

    2017  Volume 45, Issue 2, Page(s) 371–379

    Abstract: Pseudokinases and pseudophosphatases possess the ability to bind substrates without catalyzing their modification, thereby providing a mechanism to recruit potential phosphotargets away from active enzymes. Since many of these pseudoenzymes possess other ...

    Abstract Pseudokinases and pseudophosphatases possess the ability to bind substrates without catalyzing their modification, thereby providing a mechanism to recruit potential phosphotargets away from active enzymes. Since many of these pseudoenzymes possess other characteristics such as localization signals, separate catalytic sites, and protein-protein interaction domains, they have the capacity to influence signaling dynamics in local environments. In a similar manner, the targeting of signaling enzymes to subcellular locations by A-kinase-anchoring proteins (AKAPs) allows for precise and local control of second messenger signaling events. Here, we will discuss how pseudoenzymes form 'pseudoscaffolds' and compare and contrast this compartment-specific regulatory role with the signal organization properties of AKAPs. The mitochondria will be the focus of this review, as they are dynamic organelles that influence a broad range of cellular processes such as metabolism, ATP synthesis, and apoptosis.
    MeSH term(s) A Kinase Anchor Proteins/metabolism ; Animals ; Cyclic AMP/metabolism ; Humans ; Mitochondria/enzymology ; Phosphoric Monoester Hydrolases/metabolism ; Phosphotransferases/metabolism ; Protein Interaction Domains and Motifs ; Second Messenger Systems
    Chemical Substances A Kinase Anchor Proteins ; Cyclic AMP (E0399OZS9N) ; Phosphotransferases (EC 2.7.-) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
    Language English
    Publishing date 2017-04-15
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20160329
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 944: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  2. Article ; Online: Endogenous N-terminal Domain Cleavage Modulates α1D-Adrenergic Receptor Pharmacodynamics.

    Kountz, Timothy S / Lee, Kyung-Soon / Aggarwal-Howarth, Stacey / Curran, Elizabeth / Park, Ji-Min / Harris, Dorathy-Ann / Stewart, Aaron / Hendrickson, Joseph / Camp, Nathan D / Wolf-Yadlin, Alejandro / Wang, Edith H / Scott, John D / Hague, Chris

    The Journal of biological chemistry

    2016  Volume 291, Issue 35, Page(s) 18210–18221

    Abstract: The α1D-adrenergic receptor (ADRA1D) is a key regulator of cardiovascular, prostate, and central nervous system functions. This clinically relevant G protein-coupled receptor has proven difficult to study, as it must form an obligate modular homodimer ... ...

    Abstract The α1D-adrenergic receptor (ADRA1D) is a key regulator of cardiovascular, prostate, and central nervous system functions. This clinically relevant G protein-coupled receptor has proven difficult to study, as it must form an obligate modular homodimer containing the PDZ proteins scribble and syntrophin or become retained in the endoplasmic reticulum as non-functional protein. We previously determined that targeted removal of the N-terminal (NT) 79 amino acids facilitates ADRA1D plasma membrane expression and agonist-stimulated functional responses. However, whether such an event occurs in physiological contexts was unknown. Herein, we report the ADRA1D is subjected to innate NT processing in cultured human cells. SNAP near-infrared imaging and tandem-affinity purification revealed the ADRA1D is expressed as both full-length and NT truncated forms in multiple human cell lines. Serial truncation mapping identified the cleavage site as Leu(90)/Val(91) in the 95-amino acid ADRA1D NT domain, suggesting human cells express a Δ1-91 ADRA1D species. Tandem-affinity purification MS/MS and co-immunoprecipitation analysis indicate NT processing of ADRA1D is not required to form scribble-syntrophin macromolecular complexes. Yet, label-free dynamic mass redistribution signaling assays demonstrate that Δ1-91 ADRA1D agonist responses were greater than WT ADRA1D. Mutagenesis of the cleavage site nullified the processing event, resulting in ADRA1D agonist responses less than the WT receptor. Thus, we propose that processing of the ADRA1D NT domain is a physiological mechanism employed by cells to generate a functional ADRA1D isoform with optimal pharmacodynamic properties.
    MeSH term(s) Hep G2 Cells ; Humans ; MCF-7 Cells ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; PDZ Domains ; Proteolysis ; Receptors, Adrenergic, alpha-1/genetics ; Receptors, Adrenergic, alpha-1/metabolism
    Chemical Substances ADRA1D protein, human ; Neoplasm Proteins ; Receptors, Adrenergic, alpha-1
    Language English
    Publishing date 2016-07-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M116.729517
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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