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dc.contributor.authorKlenova, EMen_US
dc.contributor.authorChernukhin, IVen_US
dc.contributor.authorEl-Kady, Aen_US
dc.contributor.authorLee, REen_US
dc.contributor.authorPugacheva, EMen_US
dc.contributor.authorLoukinov, DIen_US
dc.contributor.authorGoodwin, GHen_US
dc.contributor.authorDelgado, Den_US
dc.contributor.authorFilippova, GNen_US
dc.contributor.authorLeon, Jen_US
dc.contributor.authorMorse, HCen_US
dc.contributor.authorNeiman, PEen_US
dc.contributor.authorLobanenkov, VVen_US
dc.identifier.citationMOLECULAR AND CELLULAR BIOLOGY, 2001, 21 pp. 2221 - 2234en_US
dc.description.abstractCTCF is a widely expressed and highly conserved multi-Zn-finger (ZF) nuclear factor. Binding to various CTCF target sites (CTSs) is mediated by combinatorial contributions of different ZFs. Different CTSs mediate distinct CTCF functions in transcriptional regulation, including promoter repression or activation and hormone-responsive gene silencing. In addition, the necessary and sufficient core sequences of diverse enhancer-blocking (insulator) elements, including CpG methylation-sensitive ones, have recently been pinpointed to CTSs. To determine whether a posttranslational modification may modulate CTCF functions, we studied CTCF phosphorylation. We demonstrated that most of the modifications that occur at the carboxy terminus in vivo can be reproduced in vitro with casein kinase II (CKII). Major modification sites map to four serines within the (SKKEDSSDSE)-K-604-S-609-D-610-E-612 motif that is highly conserved in vertebrates. Specific mutations of these serines abrogate phosphorylation of CTCF in vivo and CKII-induced phosphorylation in vitro. In addition, we showed that completely preventing phosphorylation by substituting all serines within this site resulted in markedly enhanced repression of the CTS-bearing vertebrate c-myc promoters, but did not alter CTCF nuclear localization or in vitro DNA-binding characteristics assayed with c-myc CTSs. Moreover, these substitutions manifested a profound effect on negative cell growth regulation by wild-type CTCF. CKII may thus be responsible for attenuation of CTCF activity, either acting on its own or by providing the signal for phosphorylation by other kinases and for CTCF-interacting protein partners.en_US
dc.format.extent2221 - 2234en_US
dc.titleFunctional phosphorylation sites in the C-terminal region of the multivalent multifunctional transcriptional factor CTCFen_US
dc.typeJournal Article
rioxxterms.typeJournal Article/Reviewen_US
pubs.notesresearcherid-numbers: Elkady, Ayman/J-5738-2012 orcid-numbers: Leon, Javier/0000-0001-5803-0112 Morse, Herbert/0000-0002-9331-3705 unique-id: ISI:000168366300030en_US
pubs.notesNot knownen_US
pubs.embargo.termsNot knownen_US
dc.contributor.icrauthorGoodwin, Grahamen_US

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