High impact information on Rala

• These results indicate that DRal regulates developmental cell shape changes through the JNK pathway [1].
• Overexpression of the wild-type DRal did not cause any visible phenotype, whereas DRal(G20V) and DRal(S25N) mutants caused defects in the development of various tissues including the cuticular surface, which is covered by parallel arrays of polarized structures such as hairs and sensory bristles [1].
• We have identified a Drosophila homologue of Ral that is widely expressed during embryogenesis and imaginal disc development [1].
• Previous studies have suggested that Ral might function to regulate the cytoskeleton; however, its in vivo function is unknown [1].
• Expression of the constitutively active DRal protein caused defects in the process of dorsal closure during embryogenesis and inhibited the phosphorylation of JNK in cultured S2 cells [1].

Biological context of Rala

• Unlike Ral and Cdc42, which are ubiquitously expressed, GEFmeso exerts distinct spatio-temporal expression patterns during embryonic development, suggesting a tissue-restricted function of the GEF in vivo [2].
• We describe the mutant alleles and mutant phenotypes of Rala and aux [3].
• Mutant alleles of clathrin heavy chain, Rala, split ends, and auxilin were identified as enhancers [3].
• The Drosophila Ral GTPase regulates developmental cell shape changes through the Jun NH(2)-terminal kinase pathway [1].
• Genetic analysis also showed that the exocyst is required for the execution of Ral function in apoptosis [4].

Anatomical context of Rala

• They reveal a signaling circuitry where Ral is functionally downstream of the Rap GTPase, at odds with the pathways described for mammalian cell lines [5].

Associations of Rala with chemical compounds

• Novel guanine nucleotide exchange factor GEFmeso of Drosophila melanogaster interacts with Ral and Rho GTPase Cdc42 [2].

Regulatory relationships of Rala

• The Ral GTPase is activated by RalGDS, which is one of the effector proteins for Ras [1].

Other interactions of Rala

• Identification and expression of Ima, a novel Ral-interacting Drosophila protein [6].
• Here we show in vitro association of GEFmeso with the GTP-bound active form of Ral and the nucleotide-free form of the Rho GTPase Cdc42 [2].
• This article reports the identification and characterization of a DBL-like guanine nucleotide exchange factor (GEF) in Drosophila, called GEFmeso, as a novel binding target of the Ras-like GTPase Ral [2].
• The mammalian Rit and Rin proteins, along with the Drosophila homologue RIC, comprise a distinct and evolutionarily conserved subfamily of Ras-related small GTP-binding proteins [7].
• Interaction of the Ras-related protein associated with diabetes rad and the putative tumor metastasis suppressor NM23 provides a novel mechanism of GTPase regulation [8].

Analytical, diagnostic and therapeutic context of Rala

• Sequence analysis of 27 alleles of each of the three Ras-related genes in Drosophila melanogaster indicates that they all have low levels of polymorphism but may experience slightly different evolutionary pressures [9].

References