Ubiquitin ligases, and uses related thereto

Details Ubiquitin ligases, and uses related thereto Ubiquitin ligases, and uses related thereto

C - Chemistry, Metallurgy

12

N

C12N 15/52 (2006.01) A01K 67/027 (2006.01) C07H 21/00 (2006.01) C12N 9/00 (2006.01) C12N 9/96 (2006.01) C12N 15/62 (2006.01) C12Q 1/25 (2006.01) C12Q 1/68 (2006.01) G01N 33/68 (2006.01)

Patent

CA 2231645

The present invention relates to the discovery in eukaryotic cells of ubiquitin ligases. These proteins are referred to herein collectively as "pub" proteins for <u>P</u>rotein <u>UB</u>iquitin ligase, and individually as h- pub1, h-pub2, h-pub3 and s-publ for the human pub1, pub2 and pub3 and Schizosaccharomyces pombe pub1 clones, repectively. Pub1 proteins apparently play a role in the ubiquitination of the mitotic activating tyrosine phosphatase cdc25, and thus they may regulate the progression of proliferation in eukaryotic cells by activating the cyclin dependent kinase complexes. In S. pombe, disruption of s-pub1 elevates the level of cdc25 protein in vivo increasing the activity of the tyrosine kinases, weel and mik1, required to arrest the cell-cycle. Loss of weel function in an S. pombe cell carrying a disruption in the s-pub1 gene results in a lethal premature entry into mitosis; such lethal phenotype can be rescued by the loss of cdc25 function. A ubiquitin thioester adduct of s-pub1 can be isolated from S. pombe and disruption of s-pub1 dramatically reduces ubiquitination of cdc25.

L'invention concerne la découverte dans ces cellules eucaryotes de d'ubiquitine ligases. Ces protéines sont désignées ici collectivement par protéines "pub" pour <u>P</u>rotein <u>(UB)</u>)iquitin ligase, et individuellement par h-pub1, h-pub2, h-pub3 et s-pub1 respectivement pour les clones des protéines humaines pub1, pub2, pub3 et pub1 de Schizosaccharomyces pombe. Les protéines pub1 jouent apparamment un rôle dans l'ubiquitination de la tyrosine phosphatase cdc25 d'activation mitotique, et peuvent ainsi réguler la progression de la prolifération dans les cellules eucaryotes par l'activation de complexes de kinases cyclinodépendantes. Dans S. pombe, la rupture de s-pub1 élève le niveau de protéine cdc25 in vivo qui augmente l'activité des tyrosine kinases, wee1 et mik1, requise pour stopper le cycle cellulaire. La perte de la fonction wee1 dans un cellule S. pombe portant une rupture dans le gène s-pub1 induit l'entrée prématurée mortelle en mitose; ce phénotype mortel peut être sauvegardé par la perte de la fonction cdc25. Un composé d'addition au thioester d'ubiquitine de s-pub1 peut être isolé de S. pombe et la rupture de s-pub1 réduit sensiblement l'ubiquitination de cdc25.

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