3ZKE

Structure of LC8 in complex with Nek9 peptide

Summary for 3ZKE

• Entry DOI: 10.2210/pdb3zke/pdb
• Related: 3ZKF
• Descriptor: DYNEIN LIGHT CHAIN 1, CYTOPLASMIC, NEK9 PROTEIN (3 entities in total)
• Functional Keywords: contractile protein-peptide complex, contractile protein/peptide
• Biological source: HOMO SAPIENS; More
• Cellular location: Cytoplasm, cytoskeleton: P63167
• Total number of polymer chains: 12
• Total formula weight: 69000.98

Authors

Gallego, P.,Velazquez-Campoy, A.,Regue, L.,Roig, J.,Reverter, D. (deposition date: 2013-01-22, release date: 2013-03-20, Last modification date: 2024-05-08)

Primary citation

Gallego, P.,Velazquez-Campoy, A.,Regue, L.,Roig, J.,Reverter, D.
Structural Analysis of the Regulation of the Dynll/Lc8 Binding to Nek9 by Phosphorylation
J.Biol.Chem., 288:12283-, 2013

PubMed Abstract: The NIMA family protein kinases Nek9/Nercc1, Nek6, and Nek7 constitute a signaling module activated in early mitosis involved in the control of spindle organization. DYNLL/LC8 (dynein light chain 8) was originally described as a component of the dynein complex, but the recent discovery of multiple interaction partners for LC8 has suggested that it has a general role as a dimerization hub that organizes different protein partners. Recent experiments suggested that LC8 binding to Nek9 was regulated by Nek9 autophosphorylation on Ser(944), a residue immediately located N-terminal to the LC8 conserved (K/R)xTQT binding motif, and that this was crucial for the control of signal transduction through the Nek/Nek6/7 module. In the present work, we present two crystal structures of LC8 with a peptide corresponding to the Nek9 binding region with and without a phosphorylation on Ser(944). Structural analysis of LC8 with both Nek9 peptides, together with different biophysical experiments, explains the observed diminished binding affinity of Nek9 to LC8 upon phosphorylation on Ser(944) within the Nek9 sequence, thus shedding light into a novel phosphorylation regulatory mechanism that interferes with LC8 protein · protein complex formation.

PubMed: 23482567
DOI: 10.1074/JBC.M113.459149

Experimental method

X-RAY DIFFRACTION (2.2 Å)