1m1l
From Proteopedia
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'''Human Suppressor of Fused (N-terminal domain)''' | '''Human Suppressor of Fused (N-terminal domain)''' | ||
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[[Category: Vos, A M.de.]] | [[Category: Vos, A M.de.]] | ||
[[Category: Wendt, U.]] | [[Category: Wendt, U.]] | ||
| - | [[Category: | + | [[Category: Fused]] |
| - | [[Category: | + | [[Category: Gene regulation]] |
| - | [[Category: | + | [[Category: Hedgehog signaling]] |
| - | [[Category: | + | [[Category: Signal transduction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:31:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:31, 2 May 2008
Human Suppressor of Fused (N-terminal domain)
Overview
The Hedgehog pathway drives proliferation and differentiation by activating the Gli/Ci family of zinc finger transcription factors. Gli/Ci proteins form Hedgehog signaling complexes with other signaling components, including the kinesin-like protein Costal-2, the serine-threonine kinase Fused, and Suppressor of Fused [Su(fu)]. In these complexes Gli/Ci proteins are regulated by cytoplasmic sequestration, phosphorylation, and proteolysis. Here we characterize structural and functional determinants of Su(fu) required for Gli regulation and show that Su(fu) contains at least two distinct domains: a highly conserved carboxy-terminal region required for binding to the amino-terminal ends of the Gli proteins and a unique amino-terminal domain that binds the carboxy-terminal tail of Gli1. While each domain is capable of binding to different Gli1 regions independently, interactions between Su(fu) and Gli1 at both sites are required for cytoplasmic tethering and repression of Gli1. Furthermore, we have solved the crystal structure of the amino-terminal domain of human Su(fu)(27-268) at 2.65 A resolution. This domain forms a concave pocket with a prominent acidic patch. Mutation at Asp(159) in the acidic patch disrupts Gli1 tethering and repression while not strongly disrupting binding, indicating that the amino-terminal domain of Su(fu) likely impacts Gli binding through a mechanism distinct from that for tethering and repression. These studies provide a structural basis for understanding the function of Su(fu).
About this Structure
1M1L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Suppressor of fused regulates Gli activity through a dual binding mechanism., Merchant M, Vajdos FF, Ultsch M, Maun HR, Wendt U, Cannon J, Desmarais W, Lazarus RA, de Vos AM, de Sauvage FJ, Mol Cell Biol. 2004 Oct;24(19):8627-41. PMID:15367681 Page seeded by OCA on Sat May 3 00:31:25 2008
