Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-6-27
pubmed:databankReference
pubmed:abstractText
We recently described the purification and cloning of extracellular signal-regulated kinase 1 (ERK1), which appears to play a pivotal role in converting tyrosine phosphorylation into the serine/threonine phosphorylations that regulate downstream events. We now describe cloning and characterization of two ERK1-related kinases, ERK2 and ERK3, and provide evidence suggesting that there are additional ERK family members. At least two of the ERKs are activated in response to growth factors; their activations correlate with tyrosine phophorylation, but also depend on additional modifications. Transcripts corresponding to the three cloned ERKs are distinctly regulated both in vivo and in a differentiating cell line. Thus, this family of kinases may serve as intermediates that depend on tyrosine phosphorylation to activate serine/threonine phosphorylation cascades. Individual family members may mediate responses in different developmental stages, in different cell types, or following exposure to different extracellular signals.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
663-75
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:2032290-Amino Acid Sequence, pubmed-meshheading:2032290-Animals, pubmed-meshheading:2032290-Astrocytes, pubmed-meshheading:2032290-Base Sequence, pubmed-meshheading:2032290-Cell Line, pubmed-meshheading:2032290-Cells, Cultured, pubmed-meshheading:2032290-Cloning, Molecular, pubmed-meshheading:2032290-Enzyme Activation, pubmed-meshheading:2032290-Hippocampus, pubmed-meshheading:2032290-Humans, pubmed-meshheading:2032290-Insulin, pubmed-meshheading:2032290-Mitogen-Activated Protein Kinase 1, pubmed-meshheading:2032290-Mitogen-Activated Protein Kinase 3, pubmed-meshheading:2032290-Mitogen-Activated Protein Kinase 6, pubmed-meshheading:2032290-Mitogen-Activated Protein Kinases, pubmed-meshheading:2032290-Molecular Sequence Data, pubmed-meshheading:2032290-Nerve Growth Factors, pubmed-meshheading:2032290-Organ Specificity, pubmed-meshheading:2032290-Phosphorylation, pubmed-meshheading:2032290-Protein Kinases, pubmed-meshheading:2032290-Pseudogenes, pubmed-meshheading:2032290-Rats, pubmed-meshheading:2032290-Recombinant Proteins, pubmed-meshheading:2032290-Sequence Homology, Nucleic Acid, pubmed-meshheading:2032290-Teratoma, pubmed-meshheading:2032290-Tyrosine
pubmed:year
1991
pubmed:articleTitle
ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF.
pubmed:affiliation
Department of Pharmacology, University of Texas Southwestern Graduate School of Biomedical Sciences, Dallas 75235-9041.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't