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  • American Association for the Advancement of Science (AAAS)  (2)
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  • American Association for the Advancement of Science (AAAS)  (2)
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  • 1
    Online Resource
    Online Resource
    A Loss-of-Function Screen Reveals Ras- and Raf-Independent MEK-ERK Signaling During Chlamydia trachomatis Infection
    American Association for the Advancement of Science (AAAS) ; 2010
    In:  Science Signaling Vol. 3, No. 113 ( 2010-03-16)
    Details
    In: Science Signaling, American Association for the Advancement of Science (AAAS), Vol. 3, No. 113 ( 2010-03-16)
    Abstract: Chlamydiae are obligate intracellular bacterial pathogens that have a major effect on human health. Because of their intimate association with their host, chlamydiae depend on various host cell functions for their survival. Here, we present an RNA-interference–based screen in human epithelial cells that identified 59 host factors that either positively or negatively influenced the replication of Chlamydia trachomatis ( Ctr ). Two factors, K-Ras and Raf-1, which are members of the canonical Ras–Raf–MEK (mitogen-activated or extracellular signal–regulated protein kinase kinase)–ERK (extracellular signal–regulated kinase) pathway, were identified as central components of signaling networks associated with hits from the screen. Depletion of Ras or Raf in HeLa cells increased pathogen growth. Mechanistic analyses revealed that ERK was activated independently of K-Ras and Raf-1. Infection with Ctr led to the Akt-dependent, increased phosphorylation (and inactivation) of Raf-1 at serine-259. Furthermore, phosphorylated Raf-1 relocalized from the cytoplasm to the intracellular bacterial inclusion in an Akt- and 14-3-3β–dependent manner. Together, these findings not only show that Chlamydia regulates components of an important host cell signaling pathway, but also provide mechanistic insights into how this is achieved.
    Type of Medium: Online Resource
    ISSN: 1945-0877 , 1937-9145
    URL: Article
    DOI: 10.1126/scisignal.2000651
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2010
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Membrane and Morphological Changes in Apoptotic Cells Regulated by Caspase-Mediated Activation of PAK2
    American Association for the Advancement of Science (AAAS) ; 1997
    In:  Science Vol. 276, No. 5318 ( 1997-06-06), p. 1571-1574
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 276, No. 5318 ( 1997-06-06), p. 1571-1574
    Abstract: Apoptosis of Jurkat T cells induced the caspase-mediated proteolytic cleavage of p21-activated kinase 2 (PAK2). Cleavage occurred between the amino-terminal regulatory domain and the carboxyl-terminal catalytic domain, which generated a constitutively active PAK2 fragment. Stable Jurkat cell lines that expressed a dominant-negative PAK mutant were resistant to the Fas-induced formation of apoptotic bodies, but had an enhanced externalization of phosphatidylserine at the cell surface. Thus, proteolytic activation of PAK2 represents a guanosine triphosphatase–independent mechanism of PAK regulation that allows PAK2 to regulate morphological changes that are seen in apoptotic cells.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.276.5318.1571
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1997
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
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    Online Resource
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