Skip to main content
The Journal of Biological Chemistry logoLink to The Journal of Biological Chemistry
. 2017 Jun 16;292(24):10316. doi: 10.1074/jbc.A116.771097

Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.

Séverine Jansen, Kateřina Melková, Zuzana Trošanová, Kateřina Hanáková, Milan Zachrdla, Jiři Nováček, Erik Župa, Zbyněk Zdráhal, Jozef Hritz, Lukáš Žídek
PMCID: PMC5473234  PMID: 28623194

VOLUME 292 (2017) PAGES 6715–6727

PAGE 6720:

There was an error in Fig. 6. Panels A and B were inadvertently exchanged. The correct legend should read as follows. Microscale thermophoretic analysis of interaction between 5 μm E52C/C348S MAP2c and 14-3-3ζ in 50 mm Tris buffer. A, phosphorylated MAP2c; B, unphosphorylated MAP2c. The plots show interactions in the 14-3-3ζ monomer concentration range from 36.6 nm to 1.2 mm. The mean values ± S.D. for each concentration point were calculated from triplicate measurements.

The results are described correctly in the text, and the error does not affect the results or conclusions of the work.


Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology

RESOURCES