pubmed-article:11830574 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C0085304 | lld:lifeskim |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C0332514 | lld:lifeskim |
pubmed-article:11830574 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
pubmed-article:11830574 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:11830574 | pubmed:dateCreated | 2002-2-6 | lld:pubmed |
pubmed-article:11830574 | pubmed:abstractText | The KH domain protein MEX-3 is central to the temporal and spatial control of PAL-1 expression in the C. elegans early embryo. PAL-1 is a Caudal-like homeodomain protein that is required to specify the fate of posterior blastomeres. While pal-1 mRNA is present throughout the oocyte and early embryo, PAL-1 protein is expressed only in posterior blastomeres, starting at the four-cell stage. To better understand how PAL-1 expression is regulated temporally and spatially, we have identified MEX-3 interacting proteins (MIPs) and characterized in detail two that are required for the patterning of PAL-1 expression. RNA interference of MEX-6, a CCCH zinc-finger protein, or SPN-4, an RNA recognition motif protein, causes PAL-1 to be expressed in all four blastomeres starting at the four-cell stage. Genetic analysis of the interactions between these mip genes and the par genes, which provide polarity information in the early embryo, defines convergent genetic pathways that regulate MEX-3 stability and activity to control the spatial pattern of PAL-1 expression. These experiments suggest that par-1 and par-4 affect distinct processes. par-1 is required for many aspects of embryonic polarity, including the restriction of MEX-3 and MEX-6 activity to the anterior blastomeres. We find that PAL-1 is not expressed in par-1 mutants, because MEX-3 and MEX-6 remain active in the posterior blastomeres. The role of par-4 is less well understood. Our analysis suggests that par-4 is required to inactivate MEX-3 at the four-cell stage. Thus, PAL-1 is not expressed in par-4 mutants because MEX-3 remains active in all blastomeres. We propose that MEX-6 and SPN-4 act with MEX-3 to translate the temporal and spatial information provided by the early acting par genes into the asymmetric expression of the cell fate determinant PAL-1. | lld:pubmed |
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pubmed-article:11830574 | pubmed:language | eng | lld:pubmed |
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pubmed-article:11830574 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11830574 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11830574 | pubmed:month | Feb | lld:pubmed |
pubmed-article:11830574 | pubmed:issn | 0950-1991 | lld:pubmed |
pubmed-article:11830574 | pubmed:author | pubmed-author:VidalMarcM | lld:pubmed |
pubmed-article:11830574 | pubmed:author | pubmed-author:HuangNancy... | lld:pubmed |
pubmed-article:11830574 | pubmed:author | pubmed-author:MootzDarcy... | lld:pubmed |
pubmed-article:11830574 | pubmed:author | pubmed-author:WalhoutAlbert... | lld:pubmed |
pubmed-article:11830574 | pubmed:author | pubmed-author:HunterCraig... | lld:pubmed |
pubmed-article:11830574 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11830574 | pubmed:volume | 129 | lld:pubmed |
pubmed-article:11830574 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11830574 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11830574 | pubmed:pagination | 747-59 | lld:pubmed |
pubmed-article:11830574 | pubmed:dateRevised | 2010-7-12 | lld:pubmed |
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pubmed-article:11830574 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11830574 | pubmed:articleTitle | MEX-3 interacting proteins link cell polarity to asymmetric gene expression in Caenorhabditis elegans. | lld:pubmed |
pubmed-article:11830574 | pubmed:affiliation | Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA. | lld:pubmed |
pubmed-article:11830574 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11830574 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:11830574 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:11830574 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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