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Drosophila 14-3-3/PAR-5 Is an Essential Mediator of PAR-1 Function in Axis Formation

Drosophila 14-3-3/PAR-5 Is an Essential Mediator of PAR-1 Function in Axis Formation

Richard Benton, Isabel M Palacios, Daniel St Johnston

Dev Cell. 2002 Nov;3(5):659-71.

PMID: 12431373

Abstract:

PAR-1 kinases are required to determine the anterior-posterior (A-P) axis in C. elegans and Drosophila, but little is known about their molecular function. We identified 14-3-3 proteins as Drosophila PAR-1 interactors and show that PAR-1 binds a domain of 14-3-3 distinct from the phosphoserine binding pocket. PAR-1 kinases phosphorylate proteins to generate 14-3-3 binding sites and may therefore directly deliver 14-3-3 to these targets. 14-3-3 mutants display identical phenotypes to par-1 mutants in oocyte determination and the polarization of the A-P axis. Together, these results indicate that PAR-1's function is mediated by the binding of 14-3-3 to its substrates. The C. elegans 14-3-3 protein, PAR-5, is also required for A-P polarization, suggesting that this is a conserved mechanism by which PAR-1 establishes cellular asymmetries.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP205383171	1,3,5-Triscarboxyphenylethynylbenzene		205383-17-1	Price

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