Skip to main content

Erratum to: In vivo role of different domains and of phosphorylation in the transcription factor Nkx2-1

The Original Article was published on 23 February 2011


After the publication of this work [1] we became aware that Panel D of Fig. 1 included an incorrect panel. In the original figure for mouse thyroid the +/ΔCOOH lane was duplicated in the +/ΔNH2 lane. The correct figure is now included in this document as Fig. 1.

Fig. 1
figure 1

Generation of mice carrying Nkx2-1 mutant alleles. (a) The structure of the Nkx2-1 mutants is schematically shown. Numbering of amino acids is shown according to [2]. P indicates phosphorylated serine residues according to [3]; AD1 and AD2, activation domains. (b) Genomic structure of the Nkx2-1 locus, wild type allele and alleles modified by homologous recombination. Black boxes represent exons; hatched box the homeobox; ATG and TGA codons are indicated. The probe used for genotyping ES cell clones and mice is indicated by a black bar labeled pr. PGKneo, selection marker; pA, SV40 poly(A) sequence; B, BamHI. (c) Southern blot analysis of genomic DNA from mouse tails digested with BamHI and probed probe within indicated in panel b. The lower band corresponds to the mutated allele (4.5 kb), the upper band to the wild type allele (12 kb). (d) Cellular extract from wild type and mutated mouse thyroids (left) were used in EMSA assays with an oligonucleotide containing a high affinity Nkx2-1 binding site. Extracts from FRTL-5 cells transfected with plasmids encoding mutated forms of Nkx2-1 were used as controls (right). Genotype of the mice and plasmids used in trasfected cells are indicated on each lane. (e) Lung homogenates (35 μg of protein) from wild type and PM/PM mice (E18.5) were phosphatase treated (+) or untreated (−), subjected to SDS PAGE, electrophoretically transferred to nitrocellulose and probed with anti Nkx2-1 antibody. The phosphate treatment increases the apparent mobility of wild type Nkx2-1 but does not affect the mobility of PM protein

We regret any inconvenience that this may have caused.


  1. Silberschmidt D, Rodriguez-Mallon A, Mithboakar P, Calì G, Amendola E, Sanges R, Zannini M, Scarfò M, De Luca P, Nitsch L, Di Lauro R, De Felice M. In vivo role of different domains and of phosphorylation in the transcription factor Nkx2-1. BMC Dev Biol. 2011;11:9.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  2. Guazzi S, Price M, De Felice M, Damante G, Mattei MG, Di Lauro R. Thyroid nuclear factor 1 (TTF-1) contains a homeodomain and displays a novel DNA binding specificity. EMBO J. 1990;9:3631–9.

    CAS  PubMed  PubMed Central  Google Scholar 

  3. Zannini MS, Acebron A, Felice MD, Arnone MI, Martin J, Santisteban P, Di Lauro R. Mapping and functional role of phosphorylation sites in the Thyroid Transcription Factor 1 (TTF-1). J Biol Chem. 1996;271:2249–54. doi:10.1074/jbc.271.4.2249.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations


Corresponding author

Correspondence to Roberto Di Lauro.

Additional information

The online version of the original article can be found under doi:10.1186/1471-213X-11-9.

Rights and permissions

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( applies to the data made available in this article, unless otherwise stated.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Silberschmidt, D., Rodriguez-Mallon, A., Mithboakar, P. et al. Erratum to: In vivo role of different domains and of phosphorylation in the transcription factor Nkx2-1. BMC Dev Biol 16, 29 (2016).

Download citation

  • Received:

  • Accepted:

  • Published:

  • DOI: