Disease relevance of VPS72

• The engineered GAP catalytic domain (GAP-344) was obtained in high yield and purity from Escherichia coli extracts by means of a single affinity column of immobilized YL1/2, eluted under mild conditions with the dipeptide, Asp-Phe [1].
• This motif is recognized by the commercially available YL1/2 monoclonal antibody to alpha-tubulin and has previously been used for the immunoaffinity purification of HIV enzymes engineered to contain this epitope (Stammers, D. K., Tisdale, M., Court, S., Parmar, V., Bradley, C., and Ross, C. K. (1991) FEBS Lett. 283, 298-302) [1].
• Forced expression of YL-1 protein suppresses the anchorage-independent growth of Kirsten sarcoma virus-transformed NIH3T3 cells [2].

High impact information on VPS72

• Here we present evidence that the YL1 protein is a previously unrecognized subunit of the TRRAP/TIP60 HAT complex [3].
• Analysis of proteins present in preparations of the TRRAP/TIP60 complex led to the identification of several new subunits, as well as several potential subunits including the YL1 protein [3].
• Gap lengths were measured from confocal microscope images of fixed spermatocytes dual labelled with 6-11B-1 to acetylated alpha-tubulin and YL1/2 to tyrosinated alpha-tubulin, the latter being used to determine the positions of kinetochores [4].
• In contrast to the suppression of anchorage-independent growth, the forced expression of YL-1 did not effect the transformed phenotypes in adherent culture and tumorigenicity in nude mice [2].
• The YL-1 gene, encoding a novel nuclear protein with transcription factor-like features, has been isolated from the human chromosome 1q21, one of the regions supposedly carrying a transformation suppressor gene(s) for Kirsten sarcoma virus-transformed NIH3T3 (DT) cells [2].

Biological context of VPS72

• These findings not only indicated that the YL-1 protein functions as a transformation suppressor, but also suggest that it may be important for elucidating anchorage independence under separate genetic control from other transformed phenotypes [2].
• Two of the ESTs correspond to the genes for YL1 and selenium-binding protein, both of which have potential tumor suppressor activity [5].
• Injection of YL1/2 prevented chromosome movement and cleavage, although the cleavage furrow developed in some cases [6].

Anatomical context of VPS72

• These results indicate that YL1/2 disassembled microtubules, whereas D2D6 did not bind to microtubules in the living cell [6].

Analytical, diagnostic and therapeutic context of VPS72

• Microinjection of the monoclonal anti-tubulin antibody YL1/2 inhibits cleavage of sand dollar eggs [6].
• The binding patterns of the two antibodies YL1/2 and TUB2.1 to the axoneme were studied by immunoblot, immunofluorescence, and immuno-electron microscopy [7].

References