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Keywords: SUMO
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Journal Articles
J Cell Sci (2022) 135 (4): jcs259449.
Published: 18 February 2022
... mRNP export. This requires the RNA-dependent ATPase activity of DDX19 and its dynamic interactions with Gle1 and Nup214. However, the regulatory mechanisms underlying these interactions are unclear. We find that DDX19 gets covalently attached with a small ubiquitin-like modifier (SUMO) at lysine 26...
Includes: Supplementary data
Journal Articles
Journal Articles
J Cell Sci (2020) 133 (14): jcs248591.
Published: 24 July 2020
... modification of KIF4A by the ubiquitin-like protein SUMO. We mapped lysine 460 in KIF4A as the SUMO acceptor site and employed CRISPR-Cas9-mediated genome editing to block SUMO conjugation of endogenous KIF4A. Failure to SUMOylate this site in KIF4A delayed cytokinesis. SUMOylation of KIF4A enhanced...
Includes: Supplementary data
Journal Articles
J Cell Sci (2019) 132 (14): jcs232330.
Published: 18 July 2019
... regulating their anaphase-specific localisation remains unknown. We have shown previously that SUMO regulates BUB-1 localisation during metaphase I. Here, we found that SUMO modification of BUB-1 is regulated by the SUMO E3 ligase GEI-17 and the SUMO protease ULP-1. SUMO and GEI-17 are required for BUB-1...
Includes: Supplementary data
Journal Articles
J Cell Sci (2019) 132 (12): jcs224501.
Published: 17 June 2019
... of the longer ridge phenotype caused by Nup358 knockdown with exogenously expressed HA–zfaPKCλ ( Fig. 3 ), 50 µM morpholino was used, and 150 µM morpholino was used for experiments shown in Figs 1 B and 4 A. Consistent with Nup358 acting as a SUMO E3 ligase for aPKC, there was a relative decrease...
Includes: Supplementary data
Journal Articles
J Cell Sci (2019) 132 (7): jcs224279.
Published: 3 April 2019
... that probably belongs to the SUMO-mediated DNA damage response pathway, both Nup2 and Nup60 show a dramatic increase in SUMOylation upon osmotic stress, with Nup2 SUMOylation being enhanced in Nup60 SUMO-deficient mutant yeast strains. Taken together, our data reveal that there are several levels of crosstalk...
Includes: Supplementary data
Journal Articles
J Cell Sci (2018) 131 (6): jcs211904.
Published: 20 March 2018
...Kathrin Kunz; Tanja Piller; Stefan Müller ABSTRACT The ubiquitin-related SUMO system controls many cellular signaling networks. In mammalian cells, three SUMO forms (SUMO1, SUMO2 and SUMO3) act as covalent modifiers of up to thousands of cellular proteins. SUMO conjugation affects cell function...
Includes: Supplementary data
Journal Articles
J Cell Sci (2017) 130 (14): 2306–2316.
Published: 15 July 2017
... (also known as TP53BP1), a mediator of the DNA damage response. Here, we provide evidence that loss of Nup153 compromises 53BP1 sumoylation, a prerequisite for efficient accumulation of 53BP1 at DSBs. Depletion of Nup153 resulted in reduced SUMO1 modification of 53BP1 and the displacement of the SUMO...
Includes: Supplementary data
Journal Articles
J Cell Sci (2016) 129 (12): 2407–2415.
Published: 15 June 2016
... initiation factors as targets for sumoylation, although in many cases the role of this modification has not been determined. We show here that eIF4A2 is modified by SUMO, with sumoylation occurring on a single residue (K226). We demonstrate that sumoylation of eIF4A2 is modestly increased in response...
Includes: Supplementary data
Journal Articles
J Cell Sci (2016) 129 (3): 580–591.
Published: 1 February 2016
... was found to associate with proteins modified by SUMO2 and/or SUMO3 in a manner dependent on its ubiquitin-binding sequences, suggesting that hybrid SUMO–ubiquitin chains can be bound. In vitro assays confirmed that RNF168, preferentially, binds hybrid SUMO2–K63 ubiquitin chains compared with K63–ubiquitin...
Includes: Supplementary data
Journal Articles
J Cell Sci (2015) 128 (10): 1934–1945.
Published: 15 May 2015
...), are often delineated by localization of adenylyl cyclase 3 (AC3, also known as ADCY3), the mechanisms responsible for targeting integral membrane proteins are largely unknown. Post-translational modification by small ubiquitin-like modifier (SUMO) proteins plays an important role in protein localization...
Includes: Supplementary data
Journal Articles
Journal Articles
J Cell Sci (2014) 127 (2): 365–375.
Published: 15 January 2014
... by the proteasome by a SUMO-dependent, ubiquitin-mediated pathway in response to arsenic treatment, curing the disease. Six major PML isoforms are expressed as a result of alternative splicing, each of which encodes a unique C-terminal region. Using a system in which only a single EYFP-linked PML isoform...
Includes: Supplementary data
Journal Articles
Journal Articles
J Cell Sci (2012) 125 (23): 5819–5829.
Published: 1 December 2012
...Raghavi Sudharsan; Yoshiaki Azuma Summary The small ubiquitin-like modifier (SUMO) ligase PIAS1 (Protein Inhibitor of Activated Stat-1) has been shown to play a role in cellular stress response by SUMOylating several proteins that are involved in DNA repair, apoptosis and transcription...
Includes: Supplementary data
Journal Articles
In collection:
Proteostasis
J Cell Sci (2012) 125 (15): 3630–3635.
Published: 1 August 2012
... and post-natal tissue homeostasis. Gene expression and function is therefore tightly controlled at a number of levels. We investigated the role that post-translational modifications play during human hepatocyte differentiation. In particular, we examined the role of the small ubiquitin-like modifier (SUMO...
Includes: Supplementary data
Journal Articles
J Cell Sci (2011) 124 (18): 3149–3163.
Published: 15 September 2011
... Transcriptional repression SUMO Accurate control of gene expression is crucial for cell survival and is clearly dependent on the chromatin status ( Narlikar et al., 2002 ). Although gene activation is generally associated with euchromatic sites with increased histone acetylation, gene inactivation...
Includes: Multimedia, Supplementary data
Journal Articles
J Cell Sci (2010) 123 (12): 2014–2024.
Published: 15 June 2010
...-independent nuclear domains (NDs) in mouse hematopoietic cells and even in Pml -deficient cells. Here, we show that MORC3 colocalizes with PML by a two-step molecular mechanism: the PML-independent formation of MORC3 NDs by the ATPase cycle, and the association of MORC3 with PML via the SUMO1-SUMO-interacting...
Includes: Supplementary data
Journal Articles
Journal Articles
J Cell Sci (2009) 122 (18): 3312–3321.
Published: 15 September 2009
... identify the SUMO E3-like ligase human polycomb protein 2 (PC2; also known as hPC2) as essential for centrin-2 modification. Interference with the SUMOylation pathway leads to a striking defect in nuclear localization of centrin-2 and accumulation in the cytoplasm, whereas centrosomal recruitment...
Includes: Supplementary data