Differential effects of Drosophila mastermind on asymmetric cell fate specification and neuroblast formation

• Published in: Genetics (Austin) Vol. 166; no. 3; pp. 1281 - 1289
• Main Authors: Yedvobnick, B, Kumar, A, Chaudhury, P, Opraseuth, J, Mortimer, N, Bhat, K.M
• Format: Journal Article
• Language: English
• Published: United States Genetics Soc America 01.03.2004; Genetics Society of America
• Subjects: Alleles; Amino Acid Sequence; Animals; Cell Lineage; Drosophila; Drosophila - embryology; Drosophila - genetics; Drosophila - physiology; Drosophila Proteins - chemistry; Drosophila Proteins - genetics; Drosophila Proteins - physiology; Epistasis, Genetic; Gene Expression Regulation, Developmental; Genotype & phenotype; Insects; Membrane Proteins - physiology; Nervous system; Neurons; Neurons - cytology; Neurons - physiology; Nuclear Proteins - chemistry; Nuclear Proteins - genetics; Nuclear Proteins - physiology; Penetrance; Proteins; Receptors, Notch
• ISSN: 0016-6731; 1943-2631; 1943-2631
• DOI: 10.1534/genetics.166.3.1281

During neurogenesis in the ventral nerve cord of the Drosophila embryo, Notch signaling participates in the pathway that mediates asymmetric fate specification to daughters of secondary neuronal precursor cells. In the NB4-2 --> GMC-1 --> RP2/sib lineage, a well-studied neuronal lineage in the ventral nerve cord, Notch signaling specifies sib fate to one of the daughter cells of GMC-1. Notch mediates this process via Mastermind (Mam). Loss of function for mam, similar to loss of function for Notch, results in GMC-1 symmetrically dividing to generate two RP2 neurons. Loss of function for mam also results in a severe neurogenic phenotype. In this study, we have undertaken a functional analysis of the Mam protein. We show that while ectopic expression of a truncated Mam protein induces a dominant-negative neurogenic phenotype, it has no effect on asymmetric fate specification. This truncated Mam protein rescues the loss of asymmetric specification phenotype in mam in an allele-specific manner. We also show an interallelic complementation of loss-of-asymmetry defect. Our results suggest that Mam proteins might associate during the asymmetric specification of cell fates and that the N-terminal region of the protein plays a role in this process.