scholarly journals Ran GTPase-Activating Protein 1

2020 ◽  
Author(s):  
Keyword(s):  
Gtpase Activating Protein ◽  
Ran Gtpase

scholarly journals Nuclear RanGAP Is Required for the Heterochromatin Assembly and Is Reciprocally Regulated by Histone H3 and Clr4 Histone Methyltransferase in Schizosaccharomyces pombe

2006 ◽  
Vol 17 (6) ◽  
pp. 2524-2536 ◽  
Author(s):  
Hitoshi Nishijima ◽  
Jun-ichi Nakayama ◽  
Tomoko Yoshioka ◽  
Ayumi Kusano ◽  
Hideo Nishitani ◽  
...  
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Histone H3 ◽  
Inhibitory Effect ◽  
Stable Complex ◽  
Gtpase Activating Protein ◽  
Ran Gtpase ◽  
The Core ◽  
Trimeric Complex ◽  
Core Histones ◽  
Heterochromatin Assembly

Although the Ran GTPase-activating protein RanGAP mainly functions in the cytoplasm, several lines of evidence indicate a nuclear function of RanGAP. We found that Schizosaccharomyces pombe RanGAP, SpRna1, bound the core of histone H3 (H3) and enhanced Clr4-mediated H3-lysine 9 (K9) methylation. This enhancement was not observed for methylation of the H3-tail containing K9 and was independent of SpRna1–RanGAP activity, suggesting that SpRna1 itself enhances Clr4-mediated H3-K9 methylation via H3. Although most SpRna1 is in the cytoplasm, some cofractionated with H3. Sprna1ts mutations caused decreases in Swi6 localization and H3-K9 methylation at all three heterochromatic regions of S. pombe. Thus, nuclear SpRna1 seems to be involved in heterochromatin assembly. All core histones bound SpRna1 and inhibited SpRna1–RanGAP activity. In contrast, Clr4 abolished the inhibitory effect of H3 on the RanGAP activity of SpRna1 but partially affected the other histones. SpRna1 formed a trimeric complex with H3 and Clr4, suggesting that nuclear SpRna1 is reciprocally regulated by histones, especially H3, and Clr4 on the chromatin to function for higher order chromatin assembly. We also found that SpRna1 formed a stable complex with Xpo1/Crm1 plus Ran-GTP, in the presence of H3.

Nuclear envelope localization of Ran-binding protein 2 and Ran-GTPase-activating protein 1 in psoriatic epidermal keratinocytes

2014 ◽  
Vol 23 (2) ◽  
pp. 119-124 ◽  
Author(s):  
Kayo Yasuda ◽  
Kazumitsu Sugiura ◽  
Takuya Takeichi ◽  
Yasushi Ogawa ◽  
Yoshinao Muro ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Binding Protein ◽  
Epidermal Keratinocytes ◽  
Gtpase Activating Protein ◽  
Ran Gtpase

scholarly journals Ran GTPase-Activating Protein 1 Is a Therapeutic Target in Diffuse Large B-Cell Lymphoma

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e79863 ◽  
Author(s):  
Kung-Chao Chang ◽  
Wei-Chao Chang ◽  
Yao Chang ◽  
Liang-Yi Hung ◽  
Chien-Hsien Lai ◽  
...  
Keyword(s):  
B Cell ◽  
Therapeutic Target ◽  
Cell Lymphoma ◽  
B Cell Lymphoma ◽  
Gtpase Activating Protein ◽  
Ran Gtpase ◽  
Large B Cell Lymphoma ◽  
Large B Cell

scholarly journals A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.

1996 ◽  
Vol 135 (6) ◽  
pp. 1457-1470 ◽  
Author(s):  
M J Matunis ◽  
E Coutavas ◽  
G Blobel
Keyword(s):  
Nuclear Pore Complex ◽  
Mitotic Spindle ◽  
Immunoblot Analysis ◽  
Peptide Sequence ◽  
Nuclear Pore ◽  
Gtpase Activating Protein ◽  
Ran Gtpase ◽  
Spindle Apparatus ◽  
Bidirectional Transport ◽  
And Function

Ran is a nuclear Ras-like GTPase that is required for the bidirectional transport of proteins and ribnucleoproteins across the nuclear pore complex (NPC). A key regulator of the Ran GTP/GDP cycle is the 70-kD Ran-GTPase-activating protein RanGAP1. Here, we report the identification and localization of a novel form of RanGAP1. Using peptide sequence analysis and specific mAbs, RanGAP1 was found to be modified by conjugation to a ubiquitin-like protein. Immunoblot analysis and immunolocalization by light and EM demonstrated that the 70-kD unmodified from of RanGAP1 is exclusively cytoplasmic, whereas the 90-kD modified form of RanGAP1 is associated with the cytoplasmic fibers of the NPC. The modified form of RanGAP1 also appeared to associated with the mitotic spindle apparatus during mitosis. These findings have specific implications for Ran function and broad implications for protein regulation by ubiquitin-like modifications. Moreover, the variety and function of ubiquitin-like protein modifications in the cell may be more diverse than previously realized.

scholarly journals Modification of Ran GTPase-activating Protein by the Small Ubiquitin-related Modifier SUMO-1 Requires Ubc9, an E2-type Ubiquitin-conjugating Enzyme Homologue

1998 ◽  
Vol 273 (11) ◽  
pp. 6503-6507 ◽  
Author(s):  
Gene W. Lee ◽  
Frauke Melchior ◽  
Michael J. Matunis ◽  
Rohit Mahajan ◽  
Qingsheng Tian ◽  
...  
Keyword(s):  
Gtpase Activating Protein ◽  
Ran Gtpase ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme
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