1WBP

SRPK1 bound to 9mer docking motif peptide

Summary for 1WBP

• Entry DOI: 10.2210/pdb1wbp/pdb
• Related: 1WAK
• Descriptor: SERINE/THREONINE-PROTEIN KINASE SPRK1, MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1, ACETATE ION, ... (4 entities in total)
• Functional Keywords: srpk, kinase, serine/threonine-protein kinase, transferase, atp-binding, chromosome partition, differentiation, mrna processing, mrna splicing, nuclear protein, nucleotide-binding, phosphorylation
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cell junction, tight junction : Q96QZ7
• Total number of polymer chains: 2
• Total formula weight: 46930.24

Authors

Ngo, J.C.,Gullinsgrud, J.,Chakrabarti, S.,Nolen, B.,Aubol, B.E.,Fu, X.-D.,Adams, J.A.,McCammon, J.A.,Ghosh, G. (deposition date: 2004-11-04, release date: 2005-10-19, Last modification date: 2023-12-13)

Primary citation

Ngo, J.C.,Chakrabarti, S.,Ding, J.-H.,Velazquez-Dones, A.,Nolen, B.,Aubol, B.E.,Adams, J.A.,Fu, X.-D.,Ghosh, G.
Interplay between Srpk and Clk/Sty Kinases in Phosphorylation of the Splicing Factor Asf/Sf2 is Regulated by a Docking Motif in Asf/Sf2
Mol.Cell, 20:77-, 2005

PubMed Abstract: 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.

PubMed: 16209947
DOI: 10.1016/J.MOLCEL.2005.08.025

Experimental method

X-RAY DIFFRACTION (2.4 Å)