Yan functions as a general inhibitor of differentiation and is negatively regulated by activation of the Ras1/MAPK pathway

Article Abstract:

Proper cell differentiation in the neuronal and nonneuronal tissues during development in Drosophila is affected by the stability of yan because it is involved in the ability of the cell to respond to inductive signals during development. Phosphorylation of the yan gene by the mitogen-activated protein kinase affects the subcellular position of yan and causes it to degrade. The yan gene inhibits cell differentiation and is an antagonist to the proneural signal which is mediated by the Ras1/MAPK pathway. Neural development is inhibited in mutants deficient in the MAPK phosphorylation site.

Cell differentiation, Phosphorylation

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PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism

Article Abstract:

Researchers have analyzed the functional relationship between the Seven In Absentia (SINA), Phyllopod (PHYL) and Tramtrack (TTK88) proteins. Particular attention was given to the regulation of TTK88 during Drosophila eye development. It was possible to establish that induction of PHYL expression prompts down-regulation of TTK88 by a process which needs SINA. TTK88 was found to be a repressor of photoreceptor cell fate determination. PHYL links with SINA to target TTK88 for degradation, thus forming a permissive environment for photoreceptor differentiation.

Metabolic regulation

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Kuzbanian controls proteolytic processing of notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis

Article Abstract:

Lateral inhibition process during Drosophila neurogenesis requires Notch and the disintegrin metalloprotease encoded by the kuzbanian (KUZ) gene. A mutant KUZ protein which lacks protease activity functions as a dominant-negative form in Drosophila. The overproduction of primary neurons resulting from lateral inhibition of Xenopus indicates an evolutionary role for KUZ. Furthermore, Notch was found to be an in vivo substrate for the KUZ protease.

Proteins, Developmental neurology, Proteolysis

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