High impact information on Hrb27C

• We identify the 50-kD protein as hrp48, a protein similar to the mammalian splicing factor hnRNP A1, and show that hrp48 recognizes specific nucleotides in a pseudo-5' splice site within the inhibitory element [1].
• The results indicate that PSI is an alternative splicing factor that regulates tissue-specific splicing, probably through interactions with generally expressed factors such as hrp48 [1].
• Previous biochemical studies have implicated hrp48 as a component of a ribonucleoprotein complex involved in the regulation of the tissue-specific alternative splicing of the P-element third intron (IVS3) [2].
• Using a P-element third-intron reporter transgene, we found that reduced levels of hrp48 partially relieve IVS3 splicing inhibition in somatic cells [2].
• Mutations in the hrp48 gene were identified and characterized. hrp48 is an essential gene [2].

Biological context of Hrb27C

• Our analyses support dual cooperative roles for Sqd, Hrb27C and Otu during Drosophila oogenesis [3].
• Dxl6 is located on the second chromosome in a position next to hrp48 and Dwee1 [4].

Anatomical context of Hrb27C

• Analysis of three hrp48 mutant alleles reveals that Hrp48 levels are crucial for polarization of the oocyte during mid-oogenesis [5].

Regulatory relationships of Hrb27C

• Our data demonstrate a novel role for Hrb27C in promoting grk localization [3].

Other interactions of Hrb27C

• We show that Sqd interacts with Hrb27C, an hnRNP previously implicated in splicing [3].
• The hrp48 alleles cause a different oskar mRNA localization defect from other mutants, and disrupt the formation of GFP-Staufen particles [6].

References