Linked Life Data

7729683

Source:http://linkedlifedata.com/resource/pubmed/id/7729683

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-6-1
pubmed:databankReference
pubmed:abstractText
Progression through the cell cycle is catalyzed by cyclin-dependent kinases (CDKs) and is negatively controlled by CDK inhibitors (CDIs). We have isolated a new member of the p21CIP1/p27KIP1 CDI family and named it p57KIP2 to denote its apparent molecular mass and higher similarity to p27KIP1. Three distinct p57 cDNAs were cloned that differ at the start of their open reading frames and correspond to messages generated by the use of distinct splice acceptor sites. p57 is distinguished from p21 and p27 by its unique domain structure. Four distinct domains follow the heterogeneous amino-terminal region and include, in order, a p21/p27-related CDK inhibitory domain, a proline-rich (28% proline) domain, an acidic (36% glutamic or aspartic acid) domain, and a carboxy-terminal nuclear targeting domain that contains a putative CDK phosphorylation site and has sequence similarity to p27 but not to p21. Most of the acidic domain consists of a novel, tandemly repeated 4-amino acid motif. p57 is a potent inhibitor of G1- and S-phase CDKs (cyclin E-cdk2, cyclin D2-cdk4, and cyclin A-cdk2) and, to lesser extent, of the mitotic cyclin B-Cdc2. In mammalian cells, p57 localizes to the nucleus, associates with G1 CDK components, and its overexpression causes a complete cell cycle arrest in G1 phase. In contrast to the widespread expression of p21 and p27 in human tissues, p57 is expressed in a tissue-specific manner, as a 1.5-kb species in placenta and at lower levels in various other tissues and a 7-kb mRNA species observed in skeletal muscle and heart. The expression pattern and unique domain structure of p57 suggest that this CDI may play a specialized role in cell cycle control.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
9
pubmed:geneSymbol
KIP2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
639-49
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7729683-Alternative Splicing, pubmed-meshheading:7729683-Amino Acid Sequence, pubmed-meshheading:7729683-Animals, pubmed-meshheading:7729683-Base Sequence, pubmed-meshheading:7729683-Cell Compartmentation, pubmed-meshheading:7729683-Cell Cycle, pubmed-meshheading:7729683-Cell Cycle Proteins, pubmed-meshheading:7729683-Cell Nucleus, pubmed-meshheading:7729683-Cloning, Molecular, pubmed-meshheading:7729683-Cyclin-Dependent Kinase Inhibitor p27, pubmed-meshheading:7729683-Cyclin-Dependent Kinase Inhibitor p57, pubmed-meshheading:7729683-Cyclin-Dependent Kinases, pubmed-meshheading:7729683-Dose-Response Relationship, Drug, pubmed-meshheading:7729683-Fungal Proteins, pubmed-meshheading:7729683-Humans, pubmed-meshheading:7729683-Mice, pubmed-meshheading:7729683-Microtubule-Associated Proteins, pubmed-meshheading:7729683-Molecular Sequence Data, pubmed-meshheading:7729683-Nuclear Proteins, pubmed-meshheading:7729683-Protein Conformation, pubmed-meshheading:7729683-Recombinant Proteins, pubmed-meshheading:7729683-S Phase, pubmed-meshheading:7729683-Sequence Homology, Amino Acid, pubmed-meshheading:7729683-Tissue Distribution, pubmed-meshheading:7729683-Tumor Suppressor Proteins
pubmed:year
1995
pubmed:articleTitle
Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution.
pubmed:affiliation
Cell Biology and Genetics Program, Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't