Twist1 dimer selection regulates cranial suture patterning and fusion.

Twist1 dimer selection regulates cranial suture patterning and fusion. Research Abstract Details 

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Twist1 dimer selection regulates cranial suture patterning and fusion. Abstract Text:

Jeannette Connerney,Viktoria Andreeva,Yael Leshem,Christian Muentener,Miguel A Mercado,Douglas B Spicer,

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.

Twist1 dimer selection regulates cranial suture patterning and fusion. Publishing Authors By Initials

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

For similar proteins: dna-binding proteins: basic helix-loop-helix transcription factors: twist transcription factor research abstracts see: proteins: dna-binding proteins: basic helix-loop-helix transcription factors: twist transcription factor research

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Twist1 dimer selection regulates cranial suture patterning and fusion. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Developmental dynamics : an official publication o

VOLUME: 235

Page Numbers: 1345-57

Journal Abbreviation: Dev. Dyn.

ISSN: 1058-8388

DAY: 3

MONTH: May

YEAR: 2006

Twist1 dimer selection regulates cranial suture patterning and fusion. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9201927

Twist1 dimer selection regulates cranial suture patterning and fusion. Keywords Mesh Terms:

KEYWORDS: Twist Transcription Factor

MESH TERMS: genetics

Chemical & Substance for Abstract: Twist1 dimer selection regulates cranial suture patterning and fusion. Information

Substance Name: Receptor, Fibroblast Growth Factor, Type

Registry Number: EC 2.7.1.112

Grant and Affiliation Information for Twist1 dimer selection regulates cranial suture patterning and fusion.

AFFILIATION: Center for Molecular Medicine, Maine Medical Center Research Institute, Scarborough, Maine 04074, USA.

Country: United States

AGENCY: United States NIDCR

GRANT: R01 DE015329

ACRONYM: DE

MEDLINETA: Dev Dyn

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