Literature DB >> 22925898

The RanBP2/RanGAP1*SUMO1/Ubc9 complex: a multisubunit E3 ligase at the intersection of sumoylation and the RanGTPase cycle.

Annette Flotho1, Andreas Werner.   

Abstract

Posttranslational modification of proteins with SUMO and the RanGTP/GDP cycle are two essential cellular mechanisms contributing directly or indirectly to almost every cellular event. The SUMO E3 ligase RanBP2 (Nup358) and the Ran GTPase activating protein (RanGAP1) are known to form a stable complex throughout the cell cycle suggesting a link between sumoylation of proteins and RanGTP hydrolysis. In a recent study we demonstrated that the stable complex of RanBP2, sumoylated RanGAP1 and Ubc9 (and not RanBP2 by itself) represents the physiologically relevant form of the SUMO ligase. Characterization of the interactions reveals an intricate proximity of two catalytic activities, sumoylation and RanGTP hydrolysis. In this ExtraView we summarize our results and discuss some ideas about a potential coupling of both processes.

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Year:  2012        PMID: 22925898      PMCID: PMC3474663          DOI: 10.4161/nucl.21980

Source DB:  PubMed          Journal:  Nucleus        ISSN: 1949-1034            Impact factor:   4.197


  31 in total

1.  Sumoylation regulates Kap114-mediated nuclear transport.

Authors:  Ute Rothenbusch; Marc Sawatzki; Yiming Chang; Stefanie Caesar; Gabriel Schlenstedt
Journal:  EMBO J       Date:  2012-05-04       Impact factor: 11.598

Review 2.  SUMOylation and deSUMOylation at a glance.

Authors:  Yonggang Wang; Mary Dasso
Journal:  J Cell Sci       Date:  2009-12-01       Impact factor: 5.285

3.  The RanBP2/RanGAP1*SUMO1/Ubc9 complex is a multisubunit SUMO E3 ligase.

Authors:  Andreas Werner; Annette Flotho; Frauke Melchior
Journal:  Mol Cell       Date:  2012-03-29       Impact factor: 17.970

Review 4.  The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.

Authors:  Jaclyn R Gareau; Christopher D Lima
Journal:  Nat Rev Mol Cell Biol       Date:  2010-12       Impact factor: 94.444

5.  The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1.

Authors:  B B Singh; H H Patel; R Roepman; D Schick; P A Ferreira
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6.  The nucleoporin Nup358/RanBP2 promotes nuclear import in a cargo- and transport receptor-specific manner.

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Journal:  PLoS Biol       Date:  2010-04-06       Impact factor: 8.029

8.  Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.

Authors:  Ali A Yunus; Christopher D Lima
Journal:  Mol Cell       Date:  2009-09-11       Impact factor: 17.970

9.  Ran-dependent docking of importin-beta to RanBP2/Nup358 filaments is essential for protein import and cell viability.

Authors:  Masakazu Hamada; Anna Haeger; Karthik B Jeganathan; Janine H van Ree; Liviu Malureanu; Sarah Wälde; Jomon Joseph; Ralph H Kehlenbach; Jan M van Deursen
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Authors:  Torsten Schaller; Karen E Ocwieja; Jane Rasaiyaah; Amanda J Price; Troy L Brady; Shoshannah L Roth; Stéphane Hué; Adam J Fletcher; KyeongEun Lee; Vineet N KewalRamani; Mahdad Noursadeghi; Richard G Jenner; Leo C James; Frederic D Bushman; Greg J Towers
Journal:  PLoS Pathog       Date:  2011-12-08       Impact factor: 6.823

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  9 in total

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Journal:  Chromosome Res       Date:  2016-01       Impact factor: 5.239

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Journal:  Bioinformatics       Date:  2015-06-10       Impact factor: 6.937

Review 5.  Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins.

Authors:  Annabel Alonso; Matt Greenlee; Jessica Matts; Jake Kline; Kayla J Davis; Rita K Miller
Journal:  Cytoskeleton (Hoboken)       Date:  2015-08-22

6.  Alterations in SUMOylation of the hyperpolarization-activated cyclic nucleotide-gated ion channel 2 during persistent inflammation.

Authors:  Lori A Forster; Leslie-Anne R Jansen; Myurajan Rubaharan; Anne Z Murphy; Deborah J Baro
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7.  Molecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells.

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  9 in total

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