» Articles » PMID: 7754385

Identification of HSRP1 Alpha As a Functional Receptor for Nuclear Localization Sequences

Overview
Journal Science
Specialty Science
Date 1995 May 19
PMID 7754385
Citations 125
Authors
Affiliations
Soon will be listed here.
Abstract

Import of proteins into the nucleus is a two-step process, involving nuclear localization sequence (NLS)-dependent docking of the substrate at the nuclear envelope followed by translocation through the nuclear pore. A recombinant human protein, hSRP1 alpha, bound in vitro specifically and directly to substrates containing either a simple or bipartite NLS motif. hSRP1 alpha promoted docking of import substrates to the nuclear envelope and together with recombinant human Ran reconstituted complete nuclear protein import. Thus, hSRP1 alpha has the properties of a cytosolic receptor for both simple and bipartite NLS motifs.

Citing Articles

Thermal Stress and Nuclear Transport.

Kose S, Ogawa Y, Imamoto N Adv Exp Med Biol. 2024; 1461:61-78.

PMID: 39289274 DOI: 10.1007/978-981-97-4584-5_5.


Karyopherins in the Remodeling of Extracellular Matrix: Implications in Tendon Injury.

Diaz C, Thankam F, Agrawal D J Orthop Sports Med. 2023; 5(3):357-374.

PMID: 37829147 PMC: 10569131. DOI: 10.26502/josm.511500122.


Henipavirus Matrix Protein Employs a Non-Classical Nuclear Localization Signal Binding Mechanism.

Donnelly C, Vogel O, Edwards M, Taylor P, Roby J, Forwood J Viruses. 2023; 15(6).

PMID: 37376602 PMC: 10303457. DOI: 10.3390/v15061302.


Distinct mutations in importin-β family nucleocytoplasmic transport receptors transportin-SR and importin-13 affect specific cargo binding.

Kimura M, Imai K, Morinaka Y, Hosono-Sakuma Y, Horton P, Imamoto N Sci Rep. 2021; 11(1):15649.

PMID: 34341383 PMC: 8329185. DOI: 10.1038/s41598-021-94948-1.


The RNA-binding protein FUS is chaperoned and imported into the nucleus by a network of import receptors.

Baade I, Hutten S, Sternburg E, Porschke M, Hofweber M, Dormann D J Biol Chem. 2021; 296:100659.

PMID: 33857479 PMC: 8131929. DOI: 10.1016/j.jbc.2021.100659.