The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. (Articolo in rivista)

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  • The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbamcr.2007.09.002 (literal)
Alternative label
  • Perconti G, Ferro A, Amato F, Rubino P, Randazzo D, Wolff T, Feo S, Giallongo A. (2007)
    The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control.
    in Biochimica et biophysica acta. Molecular cell research; Academic Press Elsevier, Amsterdam (Paesi Bassi)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Perconti G, Ferro A, Amato F, Rubino P, Randazzo D, Wolff T, Feo S, Giallongo A. (literal)
Pagina inizio
  • 1774 (literal)
Pagina fine
  • 1785 (literal)
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  • 1773 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 12 (literal)
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  • 12 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • NLM (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Oncologia Sperimentale e Applicazioni Cliniche, Università di Palermo, Italy Dipartimento Oncologico di III livello La Maddalena S.p.A., Palermo, Italy Istituto di Biomedicina e Immunologia Molecolare del Consiglio Nazionale delle Ricerche, Palermo, Italy Robert Koch Institut, Berlin, Germany (literal)
Titolo
  • The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. (literal)
Abstract
  • Alpha-enolase is a key glycolytic enzyme that plays a functional role in several physiological processes depending on the cellular localization. The enzyme is mainly localized in the cytoplasm whereas an alternative translated form, named MBP-1, is predominantly nuclear. The MBP-1 protein has been characterized as a c-Myc promoter binding protein that negatively controls transcription. In the present study, we identified the kelch protein NS1-BP as one of the alpha-enolase/MBP-1 partners by using a yeast two-hybrid screening. Although NS1-BP has been originally described as a protein mainly localized in the nucleus, we provide evidence that NS1-BP also interacts with actin in human cells, as reported for most kelch-containing proteins. Here we showed that alpha-enolase and MBP-1 associate with NS1-BP in vitro and in vivo by GST pull-down assays and coimmunoprecipitation experiments; subsequent immunofluorescent staining confirmed colocalization of the proteins within the cells. Furthermore, functional analyses performed by cotransfection assays revealed that NS1-BP enhances the inhibitory effect exerted by MBP-1 on c-Myc promoter. In mammalian cells, the overexpression of both proteins resulted in an increased repression of basal c-Myc transcription and consistently affected the steady state levels of endogenous c-Myc mRNA. These findings further support the distinct roles of alpha-enolase and its MBP-1 variant in maintaining cell homeostasis. Moreover, our data suggest a novel function for NS1-BP in the control of cell proliferation. (literal)
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