High impact information on TER94

• A number of genes known to have proteasome-related functions, including Rad23, isopeptidase T, sequestosome, and the genes for the segregase complex TER94/VCP-Ufd1-Npl4 were also found to be up-regulated [1].
• In the ex-polyQ-expressing cells of the late pupa, an upregulation of ter94 expression was observed prior to cell death [2].
• Identification of ter94, Drosophila VCP, as a modulator of polyglutamine-induced neurodegeneration [2].
• Interestingly, when ter94 was overexpressed in the eye by increasing the transgene copies, severe eye degeneration was induced [2].
• The presence of TER94 suggests that the fusome cisternae grow by vesicle fusion and are a germ cell modification of endoplasmic reticulum [3].

Biological context of TER94

• We also show that fusome association of TER94 is Bam-dependent, suggesting that cystoblast differentiation may be linked to fusome reticulum biogenesis [3].
• TER94 is expressed in embryo, in pupae and in imago, but is suppressed in larva [4].
• On the basis of its distribution we suggest that TER94 functions in the protein transport utilizing endoplasmic reticulum and Golgi derived vesicles [4].
• TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is accumulated in nonproliferating cells: in the reproductive organs and in the brain of the imago [4].
• The open reading frame of the Drosophila homolog encodes an 801 amino acid long protein (TER94), which shows high similarity to the known CDC48/p97 sequences [4].

Anatomical context of TER94

• TER94/p47 staining was observed in the nurse cells and often in the oöcytes, while TER94/p98 staining was present in the sperm bundles [4].
• Besides TER94, sex-specific forms were also detected in the gonads of the imago: p47 in the ovaries and p98 in the testis [4].

Other interactions of TER94

• We identified mutations in ter94 which disrupt the localization of oskar mRNA to the posterior pole of the oocyte [5].

References