Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5394
pubmed:dateCreated
1998-12-14
pubmed:databankReference
pubmed:abstractText
The Xenopus polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. Polo-like kinases from various organisms are activated by phosphorylation by an unidentified protein kinase. A protein kinase, polo-like kinase kinase 1 or xPlkk1, that phosphorylates and activates Plx1 in vitro was purified to near homogeneity and cloned. Phosphopeptide mapping of Plx1 phosphorylated in vitro by recombinant xPlkk1 or in progesterone-treated oocytes indicates that xPlkk1 may activate Plx1 in vivo. The xPlkk1 protein itself was also activated by phosphorylation on serine and threonine residues, and the kinetics of activation of xPlkk1 in vivo closely paralleled the activation of Plx1. Moreover, microinjection of xPlkk1 into Xenopus oocytes accelerated the timing of activation of Plx1 and the transition from G2 to M phase of the cell cycle. These results define a protein kinase cascade that regulates several events of mitosis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1701-4
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:9831560-Adenosine Triphosphate, pubmed-meshheading:9831560-Amino Acid Sequence, pubmed-meshheading:9831560-Animals, pubmed-meshheading:9831560-Catalytic Domain, pubmed-meshheading:9831560-Cell Cycle Proteins, pubmed-meshheading:9831560-Cloning, Molecular, pubmed-meshheading:9831560-Enzyme Activation, pubmed-meshheading:9831560-Mitosis, pubmed-meshheading:9831560-Molecular Sequence Data, pubmed-meshheading:9831560-Okadaic Acid, pubmed-meshheading:9831560-Oocytes, pubmed-meshheading:9831560-Peptide Mapping, pubmed-meshheading:9831560-Phosphoprotein Phosphatases, pubmed-meshheading:9831560-Phosphorylation, pubmed-meshheading:9831560-Progesterone, pubmed-meshheading:9831560-Protein-Serine-Threonine Kinases, pubmed-meshheading:9831560-Recombinant Fusion Proteins, pubmed-meshheading:9831560-Xenopus, pubmed-meshheading:9831560-Xenopus Proteins
pubmed:year
1998
pubmed:articleTitle
Purification and cloning of a protein kinase that phosphorylates and activates the polo-like kinase Plx1.
pubmed:affiliation
Howard Hughes Medical Institute and Department of Pharmacology, University of Colorado School of Medicine, Denver, Colorado 80262, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't