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Thyroid Hormones Induce Sumoylation of the Cold Shock Domain-Containing Protein PIPPin in Developing Rat Brain and in Cultured Neurons

Dipartimento di Biologia Cellulare e dello Sviluppo ‘Alberto Monroy’ (E.B., L.R., V.F., V.C.), Dipartimento Biomedico di Medicina Interna e Specialistiche (V.C., M.D.), Dipartimento di Neurologia, Oftalmologia, Otorinolaringoiatria e Psichiatria (P.P.), and Dipartimento di Scienze Biochimiche (G.S., I.D.L.), University of Palermo, 90127 Palermo, Italy

Address all correspondence and requests for reprints to: Italia Di Liegro, Dipartimento di Scienze Biochimiche, Via del Vespro 129, 90127 Palermo, Italy. E-mail: diliegro{at}unipa.it.

We previously identified a cold shock domain (CSD)-containing protein (PIPPin), expressed at high level in brain cells. PIPPin has the potential to undergo different posttranslational modifications and might be a good candidate to regulate the synthesis of specific proteins in response to extracellular stimuli. Here we report the effects of T₃ on PIPPin expression in developing rat brain. We found that a significant difference among euthyroid and hypothyroid newborn rats concerns sumoylation of nuclear PIPPin, which is abolished by hypothyroidism. Moreover, T₃ dependence of PIPPin sumoylation has been confirmed in cortical neurons purified from brain cortices and cultured in a chemically defined medium (Maat medium), with or without T₃. We also report that about one half of unmodified as well as all the sumoylated form of PIPPin could be extracted from nuclei with HCl, together with histones. Moreover, this HCl-soluble fraction remains in the nucleus even after treatment with 0.6 M KCl, thus suggesting strong interaction of PIPPin with nuclear structures and perhaps chromatin.