High impact information on cher

• The cheerio gene also encodes a new Filamin isoform that lacks the actin-binding domain [1].
• We propose that Filamin links filamentous actin to the plasma membrane of the ring canal [1].
• Furthermore, we show that Drosophila has at least two major filamin forms generated by alternative splicing from a gene that maps to position 89E10-89F4 on chromosome 3 [2].
• The longest form is enriched in the central nervous system and ovaries, shares 41.7% overall amino acid identity with human filamin (ABP-280) and contains an N-terminal actin-binding domain [2].
• These data show that Filamin function in cell motility can be provided by a truncated Filamin protein that resembles Dictyostelium Actin Binding Protein-120 [3].

Biological context of cher

• Drosophila filamin is required for follicle cell motility during oogenesis [3].
• Using the Drosophila ovary, we provide a detailed description of Filamin-deficient cells during morphogenesis [3].
• In addition, mutant follicle cell movements can be partially rescued by a transgene encoding only the actin-binding domain and the first six filamin repeats [3].
• However, follicle cell morphogenesis is unaffected by point mutations that produce truncated Filamin proteins [3].
• The Filamin family of actin binding proteins is required to maintain cell shape and promote cell locomotion [3].

Anatomical context of cher

• Expression pattern of Filamin-240 in Drosophila blood cells [4].

Other interactions of cher

• Examination of mutants in cheerio places it in the pathway of ring canal assembly between cleavage furrow arrest and localization of hts and actin filaments [5].

Analytical, diagnostic and therapeutic context of cher

• The expression pattern of Filamin-240 was studied in subsets of Drosophila blood cells by means of immunofluorescent staining and Western blot analysis with use of an antibody specific to a "filamin-folding domain", a consensus motif profile generated from the 20 existing filamin repeats [4].

References