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Title: Gli protein activity is controlled by multisite phosphorylation in vertebrate hedgehog signaling
Authors: Niewiadomski, PawelKong, Jennifer H.Ahrends, RobertMa, YanHumke, Eric W.Khan, SohiniTeruel, Mary N.Novitch, Bennett G.Rohatgi, Rajat
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Issue Date: 2013
Published in: Cell Reports, Volume 6, Issue 1, Page 168-181
Publisher: Amsterdam : Elsevier
Abstract: Gli proteins are transcriptional effectors of the Hedgehog (Hh) pathway in both normal development and cancer. We describe a program of multisite phosphorylation that regulates the conversion of Gli proteins into transcriptional activators. In the absence of Hh ligands, Gli activity is restrained by the direct phosphorylation of six conserved serine residues by protein kinase A (PKA), a master negative regulator of the Hh pathway. Activation of signaling leads to a global remodeling of the Gli phosphorylation landscape: the PKA target sites become dephosphorylated, while a second cluster of sites undergoes phosphorylation. The pattern of Gli phosphorylation can regulate Gli transcriptional activity in a graded fashion, suggesting a phosphorylation-based mechanism for how a gradient of Hh signaling in a morphogenetic field can be converted into a gradient of transcriptional activity.
Keywords: cyclic AMP dependent protein kinase; Gli protein; serine; Smoothened protein; sonic hedgehog protein; threonine; transcription factor; transcription factor Gli2; transcription factor Gli3; unclassified drug
DDC: 570
License: CC BY-NC-ND 3.0 Unported
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Appears in Collections:Biowissenschaften

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