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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 會議論文  >  Enzymology and Biology of CaaX Protein Prenylation


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81433


    Title: Enzymology and Biology of CaaX Protein Prenylation
    Authors: Fu, HW;Casey, PJ
    教師: 傅化文
    Date: 1999
    Publisher: The Endocrine Society
    Relation: Recent Progress in Hormone Research, The Endocrine Society, Volume 54, 1999, Pages 315-343
    Keywords: GERANYLGERANYLTRANSFERASE TYPE-I
    FARNESYLTRANSFERASE BETA-SUBUNIT
    FARNESYL TRANSFERASE INHIBITORS
    SWISS 3T3 CELLS
    SACCHAROMYCES-CEREVISIAE
    SUBSTRATE-BINDING
    MEVALONIC ACID
    ALPHA-SUBUNIT
    A-FACTOR
    POSTTRANSLATIONAL MODIFICATIONS
    Abstract: Protein prenylation refers to a type of lipid modification in which tither a 15-carbon farnesyl or 20-carbon geranylgeranyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins. The majority of prenylated proteins belong to a group termed "CaaX proteins" that are defined by a specific C-terminal motif that directs their modification by this process. The menage of CaaX-type prenylated proteins encompasses a wide variety of molecules that are found primarily at the cytoplasmic face of cellular membranes. These include nuclear lamins. Ras and a multitude of GTP-binding proteins (G proteins). several protein kinases and phosphatases, as well as other important proteins. A tremendous number of cellular signaling processes and regulatory events are under the control of CaaX prenyl proteins. While the attached isoprenoid lipids. in general, support the membrane association of the modified proteins, some proteins also clearly participate directly in protein-protein interactions.

    This chapter will emphasize 1) the biochemistry of the two enzymes termed farnesyltransferase and geranylgeranyltransferase type I, responsible for CaaX protein prenylation, and 2) biological roles for these modifications. Throughout. we will attempt to highlight the significance of prenylation in specific cellular events. The critical importance of this class of lipid modifications is attested to by the emergence of farnesyltransferase as a target for the development of anti-cancer therapeutics.
    Relation Link: http://www.ncbi.nlm.nih.gov/pubmed/10548882
    http://www.endocrine.org/
    URI: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81433
    Appears in Collections:[分子與細胞生物研究所] 會議論文
    [生命科學系] 會議論文

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