pop-1 encodes an HMG box protein required for the specification of a mesoderm precursor in early C. elegans embryos

Article Abstract:

The formation of mesodermal cells by the blastomeres of the precursor MS in Caenorhabditis elegans during embryogenesis requires the activity of a POP-1 protein, encoded by the pop-1 gene. The MS blastomeres of mutants containing an inactive pop-1 produce endodermal cells instead of the mesodermal cells. POP-1 contains a HMG box that binds DNA. The HMG box is similar in structure to the HMG boxes in the human T-cell factor 1 and the mouse lymphoid enhancer-binding factor 1. The MS-specific differentiation requires the interaction of POP-1 and SKN-1, encoded by the skn-1 gene.

Observations, Botany, Plant embryology

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POP-1 and anterior-posterior fate decisions in C. elegans embryos

Article Abstract:

Research was conducted to test whether the pop-1 protein gene is part of a general system for transducing data about division sequences into cell nucleus changes that affect differentiation in Caenorhabditis elegans embryos. Embryos and larvae were prepared for immunostaining by immunofluorescence while neurons were determined from hypodermal cells by morphological criteria. Results showed the presence of POP-1 asymmetry in several sequential a/p divisions and suggested that POP-1 as a part of the general a/p coordinate system that operates in the early embryo.

Physiological aspects, Genetic aspects, Cell nuclei, Cell nucleus

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WRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior polarity signals in C. elegans

Article Abstract:

A study was conducted to show that the lit-1 gene encodes a serine/threonine protein kinase homolog related to the Drosophila tissue polarity protein Nemo. The WRM-1 protein was also shown to activate the LIT-1 protein kinase during coexpression in vertebrate tissue culture cells. The activation promotes the phosphorylation of POP-1, a TCF/LEF-related protein and changes in subcellular localization.

Analysis, Cells (Biology), Cells, Drosophila, Protein kinases

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