1wbp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The arginine-serine (RS)-rich domain of the SR protein ASF/SF2 is, phosphorylated by SR protein kinases (SRPKs) and Clk/Sty kinases. However, the mode of phosphorylation by these kinases and their coordination in the, biological regulation of ASF/SF2 is unknown. Here, we report the crystal, structure of an active fragment of human SRPK1 bound to a peptide derived, from an SR protein. This structure led us to identify a docking motif in, ASF/SF2. We find that this docking motif restricts phosphorylation of, ASF/SF2 by SRPK1 to the N-terminal part of the RS domain - a property, essential for its assembly into nuclear speckles. We further show that, Clk/Sty causes release of ASF/SF2 from speckles by phosphorylating the, C-terminal part of its RS domain. These results suggest that the | + | The arginine-serine (RS)-rich domain of the SR protein ASF/SF2 is, phosphorylated by SR protein kinases (SRPKs) and Clk/Sty kinases. However, the mode of phosphorylation by these kinases and their coordination in the, biological regulation of ASF/SF2 is unknown. Here, we report the crystal, structure of an active fragment of human SRPK1 bound to a peptide derived, from an SR protein. This structure led us to identify a docking motif in, ASF/SF2. We find that this docking motif restricts phosphorylation of, ASF/SF2 by SRPK1 to the N-terminal part of the RS domain - a property, essential for its assembly into nuclear speckles. We further show that, Clk/Sty causes release of ASF/SF2 from speckles by phosphorylating the, C-terminal part of its RS domain. These results suggest that the docking, motif of ASF/SF2 is a key regulatory element for sequential, phosphorylation by SRPK1 and Clk/Sty and, thus, is essential for its, subcellular localization. |
==About this Structure== | ==About this Structure== | ||
| - | 1WBP is a | + | 1WBP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACT and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WBP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:49:23 2007'' |
Revision as of 11:44, 5 November 2007
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SRPK1 BOUND TO 9MER DOCKING MOTIF PEPTIDE
Overview
The arginine-serine (RS)-rich domain of the SR protein ASF/SF2 is, phosphorylated by SR protein kinases (SRPKs) and Clk/Sty kinases. However, the mode of phosphorylation by these kinases and their coordination in the, biological regulation of ASF/SF2 is unknown. Here, we report the crystal, structure of an active fragment of human SRPK1 bound to a peptide derived, from an SR protein. This structure led us to identify a docking motif in, ASF/SF2. We find that this docking motif restricts phosphorylation of, ASF/SF2 by SRPK1 to the N-terminal part of the RS domain - a property, essential for its assembly into nuclear speckles. We further show that, Clk/Sty causes release of ASF/SF2 from speckles by phosphorylating the, C-terminal part of its RS domain. These results suggest that the docking, motif of ASF/SF2 is a key regulatory element for sequential, phosphorylation by SRPK1 and Clk/Sty and, thus, is essential for its, subcellular localization.
About this Structure
1WBP is a Protein complex structure of sequences from Homo sapiens with ACT and ADP as ligands. Active as Transferred entry: 2.7.11.1, with EC number 2.7.1.37 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2., Ngo JC, Chakrabarti S, Ding JH, Velazquez-Dones A, Nolen B, Aubol BE, Adams JA, Fu XD, Ghosh G, Mol Cell. 2005 Oct 7;20(1):77-89. PMID:16209947
Page seeded by OCA on Mon Nov 5 13:49:23 2007
Categories: Homo sapiens | Protein complex | Transferred entry: 2.7.11.1 | Adams, J.A. | Aubol, B.E. | Chakrabarti, S. | Ding, J.H. | Fu, X.D. | Ghosh, G. | Ngo, J.C. | Nolen, B. | Velazquez-Dones, A. | ACT | ADP | Alternative splicing | Atp-binding | Chromosome partition | Differentiation | Kinase | Mrna processing | Mrna splicing | Nuclear protein | Nucleotide-binding | Phosphorylation | Serine/threonine-protein kinase | Srpk | Transferase
