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Verfasst von:Lamas, Monica [VerfasserIn]   i
 Foulkes, Nicholas S. [VerfasserIn]   i
Titel:CREM
Titelzusatz:A Master-Switch in the Transcriptional Response to cAMP
Verf.angabe:Monica Lamas, Lucia Monaco, Emmanuel Zazopoulos, Enzo Lalli, Katherine Tamai, Lucia Penna, Cristina Mazzucchelli, Francois Nantel, Nicholas S. Foulkes, Paolo Sassone-Corsi
Umfang:7 S.
Fussnoten:Gesehen am 12.06.2017
Titel Quelle:Enthalten in: Royal Society (London): Philosophical transactions of the Royal Society of London / B
Jahr Quelle:1996
Band/Heft Quelle:351(1996), 1339, S. 561-567
ISSN Quelle:2054-0280
Abstract:The CREM gene encodes both repressors and activators of cAMP-dependent transcription in a tissue and developmentally regulated manner. In addition, multiple and cooperative phosphorylation events regulate the function of the CREM proteins. CREM plays a key physiological and developmental role within the hypothalamic-pituitary axis. There is a functional switch in CREM expression during the development of male germ cells which is directed by the pituitary hormone FSH. The CREM protein in germ cells is a powerful activator which appears to function as a master-switch in the regulation of postmeiotic genes. CREM is inducible by activation of the cAMP signalling pathway with the kinetics of an early response gene. The induction is transient, cell-specific, does not involve increased transcript stability and does not require protein synthesis. The subsequent decline in CREM expression requires de novo protein synthesis. The induced transcript encodes ICER and is generated from an alternative, intronic promoter. ICER functions as a powerful repressor of cAMP-induced transcription, and represses the activity of its own promoter, thus constituting a negative autoregulatory loop.
DOI:doi:10.1098/rstb.1996.0055
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Verlag: http://dx.doi.org/10.1098/rstb.1996.0055
 Verlag: http://rstb.royalsocietypublishing.org/content/351/1339/561
 DOI: https://doi.org/10.1098/rstb.1996.0055
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1559654813
Verknüpfungen:→ Zeitschrift

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