NDLI: Distinctive phosphoinositide- and Ca2+-binding properties of normal and cognitive performance

Content Provider	Journal of Biological Chemistry (JBC)
Author	Posner, Mareike G. Upadhyay, Abhishek Ishima, Rieko Kalli, Antreas C. Harris, Gemma Kremerskothen, Joachim Sansom, Mark S. P. Crennell, Susan J. Bagby, Stefan
Abstract	Kidney- and brain-expressed protein (KIBRA), a multifunctional scaffold protein with around 20 known binding partners, is involved in memory and cognition, organ size control via the Hippo pathway, cell polarity, and membrane trafficking. KIBRA includes tandem N-terminal WW domains, a C2 domain, and motifs for binding atypical PKC and PDZ domains. A naturally occurring human KIBRA variant involving residue changes at positions 734 (Met-to-Ile) and 735 (Ser-to-Ala) within the C2 domain affects cognitive performance. We have elucidated 3D structures and calcium- and phosphoinositide-binding properties of human KIBRA C2 domain. Both WT and variant C2 adopt a canonical type I topology C2 domain fold. Neither Ca2+ nor any other metal ion was bound to WT or variant KIBRA C2 in crystal structures, and Ca2+ titration produced no significant reproducible changes in NMR spectra. NMR and X-ray diffraction data indicate that KIBRA C2 binds phosphoinositides via an atypical site involving β-strands 5, 2, 1, and 8. Molecular dynamics simulations indicate that KIBRA C2 interacts with membranes via primary and secondary sites on the same domain face as the experimentally identified phosphoinositide-binding site. Our results indicate that KIBRA C2 domain association with membranes is calcium-independent and involves distinctive C2 domain–membrane relative orientations.
Related Links	http://www.jbc.org/content/293/24/9335.abstract
Ending Page	9344
Starting Page	9335
Page Count	10
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	24
Volume Number	293
DOI	10.1074/jbc.RA118.002279
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2018-06-15
Access Restriction	Open
Subject Keyword	Nuclear magnetic resonance (NMR) Crystallography Phosphoinositide Molecular dynamics Analytical ultracentrifugation Calcium-binding protein Alzheimer disease Α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPA receptor, AMPAR) Hippo pathway Membrane trafficking C2 domain Human cognition KIBRA WWC protein family Molecular Biophysics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Trafficking of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid Receptor (AMPA) Receptor Subunit GluA2 from the Endoplasmic Reticulum Is Stimulated by a Complex Containing Ca2+/Calmodulin-activated Kinase II (CaMKII) and PICK1 Protein and by Release of Ca2+ from Internal Stores

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Cross-regulation of Phosphodiesterase 1 and Phosphodiesterase 2 Activities Controls Dopamine-mediated Striatal α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Trafficking

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Aggregation Limits Surface Expression of Homomeric GluA3 Receptors

Distinctive phosphoinositide- and Ca2+-binding properties of normal and cognitive performance–linked variant forms of KIBRA C2 domain

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