Linked Life Data

7721756

Source:http://linkedlifedata.com/resource/pubmed/id/7721756

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1995-5-19
pubmed:abstractText
Targeting of karyophilic proteins to nuclear pores is known to require several cytoplasmic factors, including the nuclear location signal-binding protein. Using a digitonin-permeabilized cell-free transport assay, we have obtained a cytoplasmic fraction containing factors that specifically bind to karyophilic protein and support the nuclear binding step of the transport. Components in this fraction form a stable complex with the karyophile through interaction with nuclear location signal. Since this complex shows nuclear pore binding activity prior to nuclear entry in the absence of other cytosolic factors, we call it nuclear pore-targeting complex. It consists of karyophilic protein and four proteins of 54, 56, 66, and 90 kDa. In our reconstitution experiments, a complex with 54 and 90 kDa proteins is capable of targeting karyophiles to the nuclear pores.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8559-65
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding.
pubmed:affiliation
Department of Anatomy and Cell Biology, Osaka University Medical School, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't