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PMID: 16502419 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Twist1 dimer selection regulates cranial suture patterning and fusion.

Connerney J, Andreeva V, Leshem Y, Muentener C, Mercado MA, Spicer DB

Abstract

Saethre-Chotzen syndrome is associated with haploinsufficiency of the basic-helix-loop-helix (bHLH) transcription factor TWIST1 and is characterized by premature closure of the cranial sutures, termed craniosynostosis; however, the mechanisms underlying this defect are unclear. Twist1 has been shown to play both positive and negative roles in mesenchymal specification and differentiation, and here we show that the activity of Twist1 is dependent on its dimer partner. Twist1 forms both homodimers (T/T) and heterodimers with E2A E proteins (T/E) and the relative level of Twist1 to the HLH inhibitor Id proteins determines which dimer forms. On the basis of the expression patterns of Twist1 and Id1 within the cranial sutures, we hypothesized that Twist1 forms homodimers in the osteogenic fronts and T/E heterodimers in the mid-sutures. In support of this hypothesis, we have found that genes regulated by T/T homodimers, such as FGFR2 and periostin, are expressed in the osteogenic fronts, whereas genes regulated by T/E heterodimers, such as thrombospondin-1, are expressed in the mid-sutures. The ratio between these dimers is altered in the sutures of Twist1+/- mice, favoring an increase in homodimers and an expansion of the osteogenic fronts. Of interest, the T/T to T/E ratio is greater in the coronal versus the sagittal suture, and this finding may contribute to making the coronal suture more susceptible to fusion due to TWIST haploinsufficiency. Importantly, we were able to inhibit suture fusion in Twist1+/- mice by modulating the balance between these dimers toward T/E formation, by either increasing the expression of E2A E12 or by decreasing Id expression. Therefore, we have identified dimer partner selection as an important mediator of Twist1 function and provide a mechanistic understanding of craniosynostosis due to TWIST haploinsufficiency.

MeSH Terms
Animals Animals, Newborn Cell Line Cranial Sutures/chemistry,embryology,growth & development Craniosynostoses/genetics,metabolism Dimerization Gene Expression Regulation, Developmental Humans Mice Mice, Inbred C3H Mice, Knockout Mice, Transgenic Nuclear Proteins/chemistry,deficiency,genetics Receptor, Fibroblast Growth Factor, Type 2/biosynthesis,genetics Twist-Related Protein 1/chemistry,deficiency,genetics
Chemicals
Nuclear Proteins Twist-Related Protein 1 Twist1 protein, mouse Receptor, Fibroblast Growth Factor, Type 2
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Connerney Jeannette
Center for Molecular Medicine, Maine Medical Center Research Institute, Scarborough, Maine 04074, USA.
Andreeva Viktoria
Leshem Yael
Muentener Christian
Mercado Miguel A
Spicer Douglas B
Article Info
Journal
Developmental dynamics : an official publication of the American Association of Anatomists
Abbr.
Dev Dyn
ISSN
1058-8388
Published
2006-05-00
Pages
1345-57
Language
English
Region
United States
NLM ID
9201927
Subset
IM
Grants
NCRR NIH HHS · P20 RR15555 · United States
NCRR NIH HHS · P20RR18789 · United States
NIDCR NIH HHS · R01 DE015329 · United States
Corrections
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