Linked Life Data

2674130

Source:http://linkedlifedata.com/resource/pubmed/id/2674130

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1989-10-25
pubmed:databankReference
pubmed:abstractText
A new family of ras-related proteins, designated rac (ras-related C3 botulinum toxin substrate) has been identified. rac1 and rac2 cDNA clones were isolated from a differentiated HL-60 library and encode proteins that are 92% homologous and share 58% and 26-30% amino acid homology with human rhos and ras, respectively. Nucleotide sequence analysis predicts both rac1 and rac2 proteins to contain 192 amino acids with molecular masses of 21,450 and 21,429 daltons, respectively. rac1 and rac2 possess four of the five conserved functional domains in ras associated with binding and hydrolysis of guanine nucleotides. They also contain the COOH-terminal consensus sequence Cys-X-X-X-COOH which localizes ras to the inner plasma membrane and the residues Gly12 and Ala59, at which sites mutations elicit transforming potential to ras. The rac transcripts, particularly rac2, display relative myeloid tissue selectivity. Both rac1 transcripts (2.4 and 1.1 kilobases (kb] increase when HL-60 cells differentiate to neutrophil-like morphology. In contrast, differentiation of U937 cells to monocyte-like morphology causes no change in the 2.4-kb mRNA and a decrease in the 1.1-kb mRNA species. rac2 mRNA (1.45 kb) increases 7-9-fold and 3-fold upon differentiation of HL-60 and U937 cells, respectively. Neither rac mRNAs are present in a Jurkat T cell line, and unlike rac1, rac2 mRNA is absent in human brain and liver tissue. Transfection experiments permitted the demonstration that rac1 and rac2 are substrates for ADP-ribosylation by the C3 component of botulinum toxin. The data suggest that racs are plasma membrane-associated GTP-binding proteins which could regulate secretory processes, particularly in myeloid cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16378-82
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:2674130-Amino Acid Sequence, pubmed-meshheading:2674130-Base Sequence, pubmed-meshheading:2674130-Botulinum Toxins, pubmed-meshheading:2674130-Cell Line, pubmed-meshheading:2674130-Cloning, Molecular, pubmed-meshheading:2674130-DNA, Neoplasm, pubmed-meshheading:2674130-Genes, ras, pubmed-meshheading:2674130-Humans, pubmed-meshheading:2674130-Leukemia, Promyelocytic, Acute, pubmed-meshheading:2674130-Molecular Sequence Data, pubmed-meshheading:2674130-Oligonucleotide Probes, pubmed-meshheading:2674130-Proteins, pubmed-meshheading:2674130-Proto-Oncogene Proteins, pubmed-meshheading:2674130-Proto-Oncogene Proteins p21(ras), pubmed-meshheading:2674130-Sequence Homology, Nucleic Acid, pubmed-meshheading:2674130-Substrate Specificity, pubmed-meshheading:2674130-rac GTP-Binding Proteins
pubmed:year
1989
pubmed:articleTitle
rac, a novel ras-related family of proteins that are botulinum toxin substrates.
pubmed:affiliation
Department of Pharmacological Sciences, Genentech, Incorporated, South San Francisco, California 94080.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.