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Sumoylation is tumor-suppressive and confers proliferative quiescence to hematopoietic progenitors in Drosophila melanogaster larvae.

Kalamarz ME, Paddibhatla I, Nadar C, Govind S.

Biol Open. 2012 Mar 15;1(3):161-72. doi: 10.1242/bio.2012043. Epub 2011 Dec 28.


The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9.

Buschmann T, Lerner D, Lee CG, Ronai Z.

J Biol Chem. 2001 Nov 2;276(44):40389-95. Epub 2001 May 30.


Alternative allosteric mechanisms can regulate the substrate and E2 in SUMO conjugation.

Karaca E, Tozluoğlu M, Nussinov R, Haliloğlu T.

J Mol Biol. 2011 Mar 4;406(4):620-30. doi: 10.1016/j.jmb.2010.12.044. Epub 2011 Jan 7.


TnaA, an SP-RING protein, interacts with Osa, a subunit of the chromatin remodeling complex BRAHMA and with the SUMOylation pathway in Drosophila melanogaster.

Monribot-Villanueva J, Juárez-Uribe RA, Palomera-Sánchez Z, Gutiérrez-Aguiar L, Zurita M, Kennison JA, Vázquez M.

PLoS One. 2013 Apr 19;8(4):e62251. doi: 10.1371/journal.pone.0062251. Print 2013.


Ubc9 sumoylation controls SUMO chain formation and meiotic synapsis in Saccharomyces cerevisiae.

Klug H, Xaver M, Chaugule VK, Koidl S, Mittler G, Klein F, Pichler A.

Mol Cell. 2013 Jun 6;50(5):625-36. doi: 10.1016/j.molcel.2013.03.027. Epub 2013 May 2.


Role for sumoylation in systemic inflammation and immune homeostasis in Drosophila larvae.

Paddibhatla I, Lee MJ, Kalamarz ME, Ferrarese R, Govind S.

PLoS Pathog. 2010 Dec 23;6(12):e1001234. doi: 10.1371/journal.ppat.1001234.


Systematic determinations of SUMOylation activation intermediates and dynamics by a sensitive and quantitative FRET assay.

Song Y, Liao J.

Mol Biosyst. 2012 Jun;8(6):1723-9. doi: 10.1039/c2mb05465e. Epub 2012 Mar 30.


Sumoylation controls retinal progenitor proliferation by repressing cell cycle exit in Xenopus laevis.

Terada K, Furukawa T.

Dev Biol. 2010 Nov 1;347(1):180-94. doi: 10.1016/j.ydbio.2010.08.023. Epub 2010 Aug 27.


Identification of a non-covalent ternary complex formed by PIAS1, SUMO1, and UBC9 proteins involved in transcriptional regulation.

Mascle XH, Lussier-Price M, Cappadocia L, Estephan P, Raiola L, Omichinski JG, Aubry M.

J Biol Chem. 2013 Dec 20;288(51):36312-27. doi: 10.1074/jbc.M113.486845. Epub 2013 Oct 30.


Performing in vitro sumoylation reactions using recombinant enzymes.

Werner A, Moutty MC, Möller U, Melchior F.

Methods Mol Biol. 2009;497:187-99. doi: 10.1007/978-1-59745-566-4_12. Review.


Sumoylation induced by the Arf tumor suppressor: a p53-independent function.

Tago K, Chiocca S, Sherr CJ.

Proc Natl Acad Sci U S A. 2005 May 24;102(21):7689-94. Epub 2005 May 16.


A mechanistic view of the role of E3 in sumoylation.

Tozluoğlu M, Karaca E, Nussinov R, Haliloğlu T.

PLoS Comput Biol. 2010 Aug 26;6(8). pii: e1000913. doi: 10.1371/journal.pcbi.1000913.


Transgenic expression of BRCA1 disturbs hematopoietic stem and progenitor cells quiescence and function.

Bai L, Shi G, Zhang X, Dong W, Zhang L.

Exp Cell Res. 2013 Oct 15;319(17):2739-46. doi: 10.1016/j.yexcr.2013.06.014. Epub 2013 Jul 10.


p21(cip1) mRNA is controlled by endogenous transforming growth factor-beta1 in quiescent human hematopoietic stem/progenitor cells.

Ducos K, Panterne B, Fortunel N, Hatzfeld A, Monier MN, Hatzfeld J.

J Cell Physiol. 2000 Jul;184(1):80-5.


The SUMO conjugating enzyme Ubc9 is required for inducing and maintaining stem cell pluripotency.

Tahmasebi S, Ghorbani M, Savage P, Gocevski G, Yang XJ.

Stem Cells. 2014 Apr;32(4):1012-20. doi: 10.1002/stem.1600.


MEL-18 interacts with HSF2 and the SUMO E2 UBC9 to inhibit HSF2 sumoylation.

Zhang J, Goodson ML, Hong Y, Sarge KD.

J Biol Chem. 2008 Mar 21;283(12):7464-9. doi: 10.1074/jbc.M707122200. Epub 2008 Jan 21.


Rhes, a physiologic regulator of sumoylation, enhances cross-sumoylation between the basic sumoylation enzymes E1 and Ubc9.

Subramaniam S, Mealer RG, Sixt KM, Barrow RK, Usiello A, Snyder SH.

J Biol Chem. 2010 Jul 2;285(27):20428-32. doi: 10.1074/jbc.C110.127191. Epub 2010 Apr 27.


Ubc9 deficiency selectively impairs the functionality of common lymphoid progenitors (CLPs) during bone marrow hematopoiesis.

Edrees MAH, Luo J, Sun F, Wang F, He L, Yue T, Chen L, Zhang J, Zhou H, Yang C, Yang P, Xiong F, Yu Q, Adam BL, Liu F, Li J, Zhang S, Wang CY.

Mol Immunol. 2019 Oct;114:314-322. doi: 10.1016/j.molimm.2019.08.003. Epub 2019 Aug 20.


Forced expression of p21 in GPIIb-p21 transgenic mice induces abnormalities in the proliferation of erythroid and megakaryocyte progenitors and primitive hematopoietic cells.

Albanese P, Chagraoui J, Charon M, Cocault L, Dusanter-Fourt I, Romeo PH, Uzan G.

Exp Hematol. 2002 Nov;30(11):1263-72.


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