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  • The human stress-activated protein kinase-interacting 1 gene encodes JNK-binding proteins.

    Author(s)
    Schroder, W
    Bushell, G
    Sculley, T
    Griffith University Author(s)
    Bushell, Gillian R.
    Schroder, Wayne
    Year published
    2005
    Metadata
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    Abstract
    The orthologous proteins of the stress-activated protein kinase-interacting 1 (Sin1) family have been implicated in several different signal transduction pathways. In this study, we have investigated the function of the full-length human Sin1 protein and a C-terminally truncated isoform, Sin1a, which is produced by alternative splicing. Immunoblot analysis using an anti-Sin1 polyclonal antibody showed that full-length Sin1 and several smaller isoforms are widely expressed. Sin1 was demonstrated to bind to c-Jun N-terminal kinase (JNK) in vitro and in vivo, while no interaction with p38- or ERK1/2-family MAPKs was observed. ...
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    The orthologous proteins of the stress-activated protein kinase-interacting 1 (Sin1) family have been implicated in several different signal transduction pathways. In this study, we have investigated the function of the full-length human Sin1 protein and a C-terminally truncated isoform, Sin1a, which is produced by alternative splicing. Immunoblot analysis using an anti-Sin1 polyclonal antibody showed that full-length Sin1 and several smaller isoforms are widely expressed. Sin1 was demonstrated to bind to c-Jun N-terminal kinase (JNK) in vitro and in vivo, while no interaction with p38- or ERK1/2-family MAPKs was observed. The Sin1a isoform could also form a complex with JNK in vivo. Despite localizing in distinct compartments within the cell, both Sin1 and Sin1a co-localized with JNK, suggesting that the Sin1 proteins could recruit JNK. Over-expression of full-length Sin1 inhibited the activation of JNK by UV-C in DG75 cells, as well as basal JNK-activity in HEK293 cells. These data suggest that the human Sin1 proteins may act as scaffold molecules in the regulation of signaling by JNK.
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    Journal Title
    Cellular Signalling
    Volume
    17
    Issue
    6
    Publisher URI
    http://www.elsevier.com/wps/find/journaldescription.cws_home/525462/description#description
    DOI
    https://doi.org/10.1016/j.cellsig.2004.10.015
    Copyright Statement
    © 2002 Elsevier : Reproduced in accordance with the copyright policy of the publisher : This journal is available online - use hypertext links
    Subject
    Biochemistry and Cell Biology
    Medical Physiology
    Publication URI
    http://hdl.handle.net/10072/4979
    Collection
    • Journal articles

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