HNF1A-MODY Mutations in Nuclear Localization Signal Impair HNF1A-Import Receptor KPNA6 Interactions

2021 ◽  
Author(s):  
Fareed M. A. Fareed ◽  
Sirin Korulu ◽  
Mehmet Özbil ◽  
Özlem Yalçın Çapan
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Localization Signal ◽  
Import Receptor

scholarly journals An epilepsy-associated mutation in the nuclear import receptor KPNA7 reduces nuclear localization signal binding

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Luke T. Oostdyk ◽  
Zhenjia Wang ◽  
Chongzhi Zang ◽  
Hui Li ◽  
Michael J. McConnell ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Nuclear Import ◽  
Nuclear Localization Signal ◽  
Localization Signal ◽  
Import Receptor

scholarly journals Coordinate Nuclear Targeting of the FANCD2 and FANCI Proteins via a FANCD2 Nuclear Localization Signal

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e81387 ◽  
Author(s):  
Rebecca A. Boisvert ◽  
Meghan A. Rego ◽  
Paul A. Azzinaro ◽  
Maurizio Mauro ◽  
Niall G. Howlett
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Nuclear Targeting ◽  
Localization Signal

scholarly journals SUMO-1 Modification and Its Role in Targeting the Ran GTPase-activating Protein, RanGAP1, to the Nuclear Pore Complex

1998 ◽  
Vol 140 (3) ◽  
pp. 499-509 ◽  
Author(s):  
Michael J. Matunis ◽  
Jian Wu ◽  
Günter Blobel
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Gtpase Activating Protein ◽  
Terminal Domain ◽  
Localization Signal

RanGAP1 is the GTPase-activating protein for Ran, a small ras-like GTPase involved in regulating nucleocytoplasmic transport. In vertebrates, RanGAP1 is present in two forms: one that is cytoplasmic, and another that is concentrated at the cytoplasmic fibers of nuclear pore complexes (NPCs). The NPC-associated form of RanGAP1 is covalently modified by the small ubiquitin-like protein, SUMO-1, and we have recently proposed that SUMO-1 modification functions to target RanGAP1 to the NPC. Here, we identify the domain of RanGAP1 that specifies SUMO-1 modification and demonstrate that mutations in this domain that inhibit modification also inhibit targeting to the NPC. Targeting of a heterologous protein to the NPC depended on determinants specifying SUMO-1 modification and also on additional determinants in the COOH-terminal domain of RanGAP1. SUMO-1 modification and these additional determinants were found to specify interaction between the COOH-terminal domain of RanGAP1 and a region of the nucleoporin, Nup358, between Ran-binding domains three and four. Together, these findings indicate that SUMO-1 modification targets RanGAP1 to the NPC by exposing, or creating, a Nup358 binding site in the COOH-terminal domain of RanGAP1. Surprisingly, the COOH-terminal domain of RanGAP1 was also found to harbor a nuclear localization signal. This nuclear localization signal, and the presence of nine leucine-rich nuclear export signal motifs, suggests that RanGAP1 may shuttle between the nucleus and the cytoplasm.

scholarly journals Definition of a major p53 binding site on Ad2E1B58K protein and a possible nuclear localization signal on the Ad12E1B54K protein

Oncogene ◽  
1999 ◽  
Vol 18 (4) ◽  
pp. 955-965 ◽  
Author(s):  
Roger JA Grand ◽  
Julian Parkhill ◽  
Tadge Szestak ◽  
Susan M Rookes ◽  
Sally Roberts ◽  
...  
Keyword(s):  
Binding Site ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Localization Signal ◽  
Definition Of
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