TY  - JOUR
A1  - Jeanclos, Elisabeth
A1  - Knobloch, Gunnar
A1  - Hoffmann, Axel
A1  - Fedorchenko, Oleg
A1  - Odersky, Andrea
A1  - Lamprecht, Anna‐Karina
A1  - Schindelin, Hermann
A1  - Gohla, Antje
T1  - Ca\(^{2+}\) functions as a molecular switch that controls the mutually exclusive complex formation of pyridoxal phosphatase with CIB1 or calmodulin
JF  - FEBS Letters
N2  - Pyridoxal 5′‐phosphate (PLP) is an essential cofactor for neurotransmitter metabolism. Pyridoxal phosphatase (PDXP) deficiency in mice increases PLP and γ‐aminobutyric acid levels in the brain, yet how PDXP is regulated is unclear. Here, we identify the Ca\(^{2+}\)‐ and integrin‐binding protein 1 (CIB1) as a PDXP interactor by yeast two‐hybrid screening and find a calmodulin (CaM)‐binding motif that overlaps with the PDXP‐CIB1 interaction site. Pulldown and crosslinking assays with purified proteins demonstrate that PDXP directly binds to CIB1 or CaM. CIB1 or CaM does not alter PDXP phosphatase activity. However, elevated Ca\(^{2+}\) concentrations promote CaM binding and, thereby, diminish CIB1 binding to PDXP, as both interactors bind in a mutually exclusive way. Hence, the PDXP‐CIB1 complex may functionally differ from the PDXP‐Ca\(^{2+}\)‐CaM complex.
KW  - calmodulin
KW  - chronophin
KW  - CIB1
KW  - haloacid dehalogenase
KW  - pyridoxal phosphatase
KW  - vitamin B6
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-217963
VL  - 594
IS  - 13
SP  - 2099
EP  - 2115
ER  -