Linked Life Data

11688563

Source:http://linkedlifedata.com/resource/pubmed/id/11688563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2001-11-1
pubmed:abstractText
The basic helix-loop-helix transcription factor Twist regulates a series of distinct cell fate decisions within the Drosophila mesodermal lineage. These twist functions are reflected in its dynamic pattern of expression, which is characterized by initial uniform expression during mesoderm induction, followed by modulated expression at high and low levels in each mesodermal segment, and finally restricted expression in adult muscle progenitors. We show two distinct partner-dependent functions for Twist that are crucial for cell fate choice. We find that Twist can form homodimers and heterodimers with the Drosophila E protein homologue, Daughterless, in vitro. Using tethered dimers to assess directly the function of these two particular dimers in vivo, we show that Twist homodimers specify mesoderm and the subsequent allocation of mesodermal cells to the somatic muscle fate. Misexpression of Twist-tethered homodimers in the ectoderm or mesoderm leads to ectopic somatic muscle formation overriding other developmental cell fates. In addition, expression of tethered Twist homodimers in embryos null for twist can rescue mesoderm induction as well as somatic muscle development. Loss of function analyses, misexpression and dosage experiments, and biochemical studies indicate that heterodimers of Twist and Daughterless repress genes required for somatic myogenesis. We propose that these two opposing roles explain how modulated Twist levels promote the allocation of cells to the somatic muscle fate during the subdivision of the mesoderm. Moreover, this work provides a paradigm for understanding how the same protein controls a sequence of events within a single lineage.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0950-1991
pubmed:author
pubmed:issnType
Print
pubmed:volume
128
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3145-59
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11688563-Animals, pubmed-meshheading:11688563-Basic Helix-Loop-Helix Transcription Factors, pubmed-meshheading:11688563-Binding Sites, pubmed-meshheading:11688563-Cell Lineage, pubmed-meshheading:11688563-Cells, Cultured, pubmed-meshheading:11688563-DNA, pubmed-meshheading:11688563-DNA, Complementary, pubmed-meshheading:11688563-DNA-Binding Proteins, pubmed-meshheading:11688563-Dimerization, pubmed-meshheading:11688563-Drosophila, pubmed-meshheading:11688563-Drosophila Proteins, pubmed-meshheading:11688563-Immunohistochemistry, pubmed-meshheading:11688563-Mesoderm, pubmed-meshheading:11688563-Models, Genetic, pubmed-meshheading:11688563-Muscles, pubmed-meshheading:11688563-Nuclear Proteins, pubmed-meshheading:11688563-Protein Binding, pubmed-meshheading:11688563-Protein Structure, Tertiary, pubmed-meshheading:11688563-Transcription Factors, pubmed-meshheading:11688563-Transfection, pubmed-meshheading:11688563-Twist Transcription Factor
pubmed:year
2001
pubmed:articleTitle
Dimerization partners determine the activity of the Twist bHLH protein during Drosophila mesoderm development.
pubmed:affiliation
Program in Molecular Biology, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't