Publication Date:
1992-01-10
Description:
Mitogen-activated protein (MAP) kinases are activated in response to a variety of extracellular stimuli by phosphorylation on tyrosine and threonine residues. Xp42 is a Xenopus laevis MAP kinase that is activated during oocyte maturation. Modified forms of Xp42 that lacked enzymatic activity or either of the phosphorylation sites were expressed in Xenopus oocytes. When meiotic maturation was induced with progesterone, each mutant Xp42 was phosphorylated, indicating that at least one kinase was activated that can phosphorylate Xp42 on tyrosine and threonine. Phosphorylation of one residue is not strictly dependent on phosphorylation of the other.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Posada, J -- Cooper, J A -- CA-08860/CA/NCI NIH HHS/ -- CA-28151/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):212-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1313186" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Calcium-Calmodulin-Dependent Protein Kinases
;
Enzyme Activation
;
Female
;
Glutathione Transferase/genetics/metabolism
;
Meiosis/*physiology
;
Methionine/metabolism
;
Mitogen-Activated Protein Kinase 1
;
Molecular Sequence Data
;
Oocytes/cytology/drug effects/*enzymology
;
Peptides/chemical synthesis/metabolism
;
Phosphates/metabolism
;
Phosphorylation
;
Progesterone/pharmacology
;
Protein Kinases/genetics/isolation & purification/*metabolism
;
Protein-Serine-Threonine Kinases
;
Protein-Tyrosine Kinases
;
Proto-Oncogene Proteins c-myc/genetics/metabolism
;
RNA, Messenger/genetics
;
Recombinant Fusion Proteins/metabolism
;
Transcription, Genetic
;
Xenopus laevis
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
