Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPP in developing rat brain and in cultured neurons.

Italia Di Liegro, Maria Donatelli, Patrizia Proia, Gabriella Schiera, Italia Di Liegro, Valentina Favaloro, Vincenza Compagno

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Abstract

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 post-translational 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 thyroid hormone (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, that 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, MM), 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.
Lingua originaleEnglish
pagine (da-a)252-257
Numero di pagine6
RivistaEndocrinology
Volume148
Stato di pubblicazionePublished - 2007

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Sumoylation
Thyroid Hormones
Shock
Neurons
Brain
Triiodothyronine
Post Translational Protein Processing
Hypothyroidism
Histones
Chromatin
Protein Domains
Proteins

All Science Journal Classification (ASJC) codes

  • Endocrinology

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title = "Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPP in developing rat brain and in cultured neurons.",
abstract = "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 post-translational 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 thyroid hormone (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, that 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, MM), 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.",
author = "{Di Liegro}, Italia and Maria Donatelli and Patrizia Proia and Gabriella Schiera and {Di Liegro}, Italia and Valentina Favaloro and Vincenza Compagno",
year = "2007",
language = "English",
volume = "148",
pages = "252--257",
journal = "Endocrinology",
issn = "0013-7227",
publisher = "The Endocrine Society",

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TY - JOUR

T1 - Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPP in developing rat brain and in cultured neurons.

AU - Di Liegro, Italia

AU - Donatelli, Maria

AU - Proia, Patrizia

AU - Schiera, Gabriella

AU - Di Liegro, Italia

AU - Favaloro, Valentina

AU - Compagno, Vincenza

PY - 2007

Y1 - 2007

N2 - 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 post-translational 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 thyroid hormone (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, that 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, MM), 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.

AB - 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 post-translational 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 thyroid hormone (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, that 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, MM), 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.

UR - http://hdl.handle.net/10447/6277

M3 - Article

VL - 148

SP - 252

EP - 257

JO - Endocrinology

JF - Endocrinology

SN - 0013-7227

ER -