2015
DOI: 10.1073/pnas.1505995112
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Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation

Abstract: Ran is a small GTP-binding protein of the Ras superfamily regulating fundamental cellular processes: nucleo-cytoplasmic transport, nuclear envelope formation and mitotic spindle assembly. An intracellular Ran•GTP/Ran•GDP gradient created by the distinct subcellular localization of its regulators RCC1 and RanGAP mediates many of its cellular effects. Recent proteomic screens identified five Ran lysine acetylation sites in human and eleven sites in mouse/rat tissues. Some of these sites are located in functional… Show more

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Cited by 72 publications
(93 citation statements)
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“…Emerging results suggest that inhibiting AURKA may be a novel strategy for reducing the stability of Myc protein that has not been previously targetable. Ras‐related nuclear protein (RAN) is a well‐known nuclear trafficking protein that is a member of the Ras family 18. RAN is overexpressed in diverse malignancies and promotes AURKA phosphorylation.…”
Section: Introductionmentioning
confidence: 99%
“…Emerging results suggest that inhibiting AURKA may be a novel strategy for reducing the stability of Myc protein that has not been previously targetable. Ras‐related nuclear protein (RAN) is a well‐known nuclear trafficking protein that is a member of the Ras family 18. RAN is overexpressed in diverse malignancies and promotes AURKA phosphorylation.…”
Section: Introductionmentioning
confidence: 99%
“…Known interactors of RAN are among the top identified proteins in our data set. This includes XPO5, XOP7, RanGNRF, its deacetylase sirtuin‐2 (de Boor et al , 2015), IPO9, XPO1, RANBP1, and IPO7 that all are among the top 20 identified proteins in this order. We believe that the RAN data sets will also contain many export cargos of NTRs not targeted in this study because RAN is part of the respective export complexes and interacted with various exportins in our data.…”
Section: Discussionmentioning
confidence: 99%
“…Recent work from Mann and colleagues (45) identified phosphorylation by LRRK2 of the switch II regions of Rab3a, Rab8a, Rab10, and Rab12 as a driver of membrane localization. In addition, a few GTPases outside the Rab family, including Cdc42, Rac1, and Ran, are thought to be regulated by modification of switch II (46)(47)(48). Switch II has long been recognized for its importance in dictating the Rab activation state; it has now becoming clear that posttranslational modification of this region allows further, external control of Rab function.…”
Section: Discussionmentioning
confidence: 99%