Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2001-10-29
pubmed:abstractText
The ubiquitin-conjugating enzyme, CDC34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(Kip1), IkappaBalpha, Wee1, and MyoD. We show that mammalian CDC34 is a phosphoprotein that is phosphorylated in proliferating cells. By yeast two-hybrid screening, we identified the regulatory (beta) subunit of human casein kinase 2 (CK2) as a CDC34-interacting protein and show that human CDC34 interacts in vivo with CK2beta in transfected cells. CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. Importantly, this phosphorylation is inhibited by heparin, a substrate-specific inhibitor of CK2. We have also identified a kinase activity associated with CDC34 in proliferating cells, and we show that this kinase is sensitive to heparin and can utilize GTP, strongly suggesting it is CK2. Phosphorylation of CDC34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of CDC34 at CK2-targeted residues, Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, abolishes the phosphorylation of CDC34 observed in vivo and markedly shifts nuclearly localized CDC34 to the cytoplasm. These results suggest a potential role for CK2-mediated phosphorylation in the regulation of CDC34 cell localization and function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinase II, http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Heparin, http://linkedlifedata.com/resource/pubmed/chemical/Ligases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases, http://linkedlifedata.com/resource/pubmed/chemical/anaphase-promoting complex
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41049-58
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11546811-Amino Acid Sequence, pubmed-meshheading:11546811-Animals, pubmed-meshheading:11546811-Casein Kinase II, pubmed-meshheading:11546811-Cell Division, pubmed-meshheading:11546811-Cell Extracts, pubmed-meshheading:11546811-Enzyme Inhibitors, pubmed-meshheading:11546811-Guanosine Triphosphate, pubmed-meshheading:11546811-HeLa Cells, pubmed-meshheading:11546811-Heparin, pubmed-meshheading:11546811-Humans, pubmed-meshheading:11546811-Ligases, pubmed-meshheading:11546811-Mice, pubmed-meshheading:11546811-Mice, Transgenic, pubmed-meshheading:11546811-Molecular Sequence Data, pubmed-meshheading:11546811-Phosphorylation, pubmed-meshheading:11546811-Protein-Serine-Threonine Kinases, pubmed-meshheading:11546811-Recombinant Proteins, pubmed-meshheading:11546811-Substrate Specificity, pubmed-meshheading:11546811-Transfection, pubmed-meshheading:11546811-Two-Hybrid System Techniques, pubmed-meshheading:11546811-Ubiquitin-Protein Ligase Complexes, pubmed-meshheading:11546811-Ubiquitin-Protein Ligases
pubmed:year
2001
pubmed:articleTitle
Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2.
pubmed:affiliation
Department of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245-3207, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't