Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-10-13
pubmed:abstractText
Reversible protein phosphorylation is an important mode of regulation of cellular processes. While earlier studies focused on protein kinases, it is now apparent that protein phosphatases play an equally integral role in the control of cellular phosphoproteins. This review examines the role played by endogenous inhibitors of three major protein serine/threonine phosphatases, PP1, PP2A and PP2B in the control of cell physiology. The discussion highlights novel paradigms for signal transduction by protein phosphatase inhibitors that provide important avenues for signal amplification, the timing of physiological responses and cross-talk between distinct signal transduction pathways. New evidence also points to genetic abnormalities or altered expression of phosphatase inhibitors as potential mechanisms for human disease.Together, the data emphasize the physiological importance of protein phosphatase inhibitors and establish phosphatase regulation as a key feature of hormone signaling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dopamine and cAMP-Regulated..., http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Glycogen, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PPP1R8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase inhibitor-1, http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase inhibitor-2
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1093-4715
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
D961-72
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9727084-Animals, pubmed-meshheading:9727084-Calcineurin, pubmed-meshheading:9727084-Carrier Proteins, pubmed-meshheading:9727084-Cell Division, pubmed-meshheading:9727084-Disease, pubmed-meshheading:9727084-Dopamine and cAMP-Regulated Phosphoprotein 32, pubmed-meshheading:9727084-Endoribonucleases, pubmed-meshheading:9727084-Enzyme Inhibitors, pubmed-meshheading:9727084-Glycogen, pubmed-meshheading:9727084-Humans, pubmed-meshheading:9727084-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:9727084-Muscle Contraction, pubmed-meshheading:9727084-Nerve Tissue Proteins, pubmed-meshheading:9727084-Neuronal Plasticity, pubmed-meshheading:9727084-Phosphoprotein Phosphatases, pubmed-meshheading:9727084-Phosphoproteins, pubmed-meshheading:9727084-Phosphorylation, pubmed-meshheading:9727084-Proteins, pubmed-meshheading:9727084-RNA-Binding Proteins
pubmed:year
1998
pubmed:articleTitle
Physiologic importance of protein phosphatase inhibitors.
pubmed:affiliation
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
pubmed:publicationType
Journal Article, Review