Publikationsdatum:
1990-12-14
Beschreibung:
The onset of M phase requires the activation of the pp34 protein kinase in all eukaryotes thus far examined. In Schizosaccharomyces pombe, pp34 is phosphorylated on Tyr15, and dephosphorylation of this residue regulates the initiation of mitosis. In this study, it is shown that dephosphorylation of Tyr15 triggered activation of the pp34-cyclin complex from fission yeast, that a human protein-tyrosine phosphatase can catalyze this event both in vitro and in vivo, and that activation of fission yeast pp34 does not require threonine dephosphorylation. The complementary DNA that encoded the tyrosine phosphatase replaced the mitotic activator p80cdc25, closely associating the cdc25(+)-activating pathway with tyrosine dephosphorylation of pp34.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gould, K L -- Moreno, S -- Tonks, N K -- Nurse, P -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Oxford, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1703321" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
*Cell Cycle Proteins
;
Cyclins/metabolism
;
Enzyme Activation
;
Fungal Proteins/*metabolism
;
Humans
;
*Mitosis
;
Mutation
;
Phosphoprotein Phosphatases/genetics/*metabolism
;
Phosphorylation
;
Phosphotyrosine
;
Protein Kinases/*metabolism
;
Protein Tyrosine Phosphatases
;
Schizosaccharomyces/genetics/*metabolism
;
Transformation, Genetic
;
Tyrosine/analogs & derivatives/metabolism
;
*ras-GRF1
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
Permalink
