<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Riddick G</submitter><funding>NCRR NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>118</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC1911202</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>3</volume><pubmed_abstract>Although there exists a large family of nuclear transport receptors (Karyopherins), the majority of known import cargoes use an adapter protein, Importin-alpha (Impalpha), which links the cargo to a karyopherin, Importin-beta (Impbeta). The reason for the existence of transport adapters is unknown. One hypothesis is that, as Impalpha re-export is coupled to GTP hydrolysis, it can drive a higher concentration of nuclear cargo than could be achieved by direct cargo binding to Importin-beta. However, computer simulations predicted the opposite outcome, and showed that direct transport is faster than adapter-mediated transport. These predictions were validated experimentally. The data, together with previous analyses of nuclear protein import, suggest that the use of adapters such as importin-alpha provides the cell with increased dynamic range for control of nuclear import rates, but at the expense of efficiency.</pubmed_abstract><journal>Molecular systems biology</journal><pubmed_title>The adapter importin-alpha provides flexible control of nuclear import at the expense of efficiency.</pubmed_title><pmcid>PMC1911202</pmcid><funding_grant_id>U54 RR022232</funding_grant_id><funding_grant_id>R01 GM050526</funding_grant_id><funding_grant_id>GM50525</funding_grant_id><funding_grant_id>U54 RR 022232</funding_grant_id><pubmed_authors>Riddick G</pubmed_authors><pubmed_authors>Macara IG</pubmed_authors></additional><is_claimable>false</is_claimable><name>The adapter importin-alpha provides flexible control of nuclear import at the expense of efficiency.</name><description>Although there exists a large family of nuclear transport receptors (Karyopherins), the majority of known import cargoes use an adapter protein, Importin-alpha (Impalpha), which links the cargo to a karyopherin, Importin-beta (Impbeta). The reason for the existence of transport adapters is unknown. One hypothesis is that, as Impalpha re-export is coupled to GTP hydrolysis, it can drive a higher concentration of nuclear cargo than could be achieved by direct cargo binding to Importin-beta. However, computer simulations predicted the opposite outcome, and showed that direct transport is faster than adapter-mediated transport. These predictions were validated experimentally. The data, together with previous analyses of nuclear protein import, suggest that the use of adapters such as importin-alpha provides the cell with increased dynamic range for control of nuclear import rates, but at the expense of efficiency.</description><dates><release>2007-01-01T00:00:00Z</release><publication>2007</publication><modification>2025-04-19T13:09:51.041Z</modification><creation>2019-03-27T02:04:18Z</creation></dates><accession>S-EPMC1911202</accession><cross_references><pubmed>17551513</pubmed><doi>10.1038/msb4100160</doi></cross_references></HashMap>