Publication Date:
1996-10-25
Description:
A cytosolic yeast karyopherin, Kap104p, was isolated and shown to function in the nuclear import of a specific class of proteins. The protein bound directly to repeat-containing nucleoporins and to a cytosolic pool of two nuclear messenger RNA (mRNA) binding proteins, Nab2p and Nab4p. Depletion of Kap104p resulted in a rapid shift of Nab2p from the nucleus to the cytoplasm without affecting the localization of other nuclear proteins tested. This finding suggests that the major function of Kap104p lies in returning mRNA binding proteins to the nucleus after mRNA export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aitchison, J D -- Blobel, G -- Rout, M P -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):624-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. blobel@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849456" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Biological Transport
;
Carrier Proteins/chemistry/isolation & purification/*metabolism
;
Cell Nucleus/*metabolism
;
Cytosol/chemistry/metabolism
;
Fungal Proteins/*metabolism
;
*Karyopherins
;
Membrane Proteins/metabolism
;
Molecular Sequence Data
;
Mutation
;
Nuclear Envelope/metabolism
;
*Nuclear Pore Complex Proteins
;
Nuclear Proteins/*metabolism
;
*Nucleocytoplasmic Transport Proteins
;
RNA, Messenger/genetics/metabolism
;
RNA-Binding Proteins/*metabolism
;
Recombinant Fusion Proteins/metabolism
;
Saccharomyces cerevisiae/*metabolism
;
*Saccharomyces cerevisiae Proteins
;
Temperature
;
beta Karyopherins
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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