Lamin A reassembly at the end of mitosis is regulated by its SUMO-interacting motif

Moriuchi, Takanobu; Kuroda, Masaki; Kusumoto, Fumiya; Osumi, Takashi; Hirose, Fumiko

doi:10.1016/j.yexcr.2016.02.016

Cited by 25 publications

(30 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Importantly, through reciprocal immunoprecipitation assays using cell lysates expressing BAF-WT and BAF-K6R, we found that the binding of BAF-K6R to lamin A/C was severely reduced ( These data suggest that the interaction between lamin A/C and BAF is dependent on BAF K6 SUMOylation. To confirm this, we generated a panel of GFP-tagged SIM-defective lamin A mutants, SIM1(EE) to SIM4(EE) (35), and individually coexpressed them with Myc-BAF in cells. Interactions between BAF and the SIM-deficient lamin A mutants were decreased compared with WT lamin A (Fig.…”

Section: Resultsmentioning

confidence: 99%

K6-linked SUMOylation of BAF regulates nuclear integrity and DNA replication in mammalian cells

Lin

Wang

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Barrier-to-autointegration factor (BAF) is a highly conserved protein in metazoans that has multiple functions during the cell cycle. We found that BAF is SUMOylated at K6, and that this modification is essential for its nuclear localization and function, including nuclear integrity maintenance and DNA replication. K6-linked SUMOylation of BAF promotes binding and interaction with lamin A/C to regulate nuclear integrity. K6-linked SUMOylation of BAF also supports BAF binding to DNA and proliferating cell nuclear antigen and regulates DNA replication. SENP1 and SENP2 catalyze the de-SUMOylation of BAF at K6. Disrupting the SUMOylation and de-SUMOylation cycle of BAF at K6 not only disturbs nuclear integrity, but also induces DNA replication failure. Taken together, our findings demonstrate that SUMOylation at K6 is an important regulatory mechanism that governs the nuclear functions of BAF in mammalian cells.

show abstract

Section: Resultsmentioning

confidence: 99%

K6-linked SUMOylation of BAF regulates nuclear integrity and DNA replication in mammalian cells

Lin

Wang

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…For most of the other post-translational modifications of lamins, the functional implications remain unclear (Simon and Wilson, 2013). Sumoylation at Lys201 affects lamin A localization and assembly (Zhang and Sarge, 2008), and a SUMO-interacting motif in the lamin A IgG-fold that might mediate interaction with other sumoylated proteins is required for postmitotic dephosphorylation of lamin A and its accumulation on chromosomes (Moriuchi et al, 2016).…”

Section: Regulation Of A-type Lamins In the Nuclear Interiormentioning

confidence: 99%

Lamins in the nuclear interior − life outside the lamina

Naetar

Ferraioli

Foisner

2017

Journal of Cell Science

148

136

View full text Add to dashboard Cite

Nuclear lamins are components of the peripheral lamina that define the mechanical properties of nuclei and tether heterochromatin to the periphery. A-type lamins localize also to the nuclear interior, but the regulation and specific functions of this nucleoplasmic lamin pool are poorly understood. In this Commentary, we summarize known pathways that are potentially involved in the localization and dynamic behavior of intranuclear lamins, including their post-translational modifications and interactions with nucleoplasmic proteins, such as lamina-associated polypeptide 2α (LAP2α; encoded by ). In addition, new data suggest that lamins in the nuclear interior have an important role in chromatin regulation and gene expression through dynamic binding to both hetero- and euchromatic genomic regions and promoter subdomains, thereby affecting epigenetic pathways and chromatin accessibility. Nucleoplasmic lamins also have a role in spatial chromatin organization and may be involved in mechanosignaling. In view of this newly emerging concept, we propose that the previously reported cellular phenotypes in lamin-linked diseases are, at least in part, rooted in an impaired regulation and/or function of the nucleoplasmic lamin A/C pool.

show abstract

“…A subset of FPLD cases, also called Dunnigan-type familial partial lipodystrophy, or familial partial lipodystrophy type 2 (FPLD2), is caused by mutations in LMNA gene encoding structural nuclear proteins Lamin A and C (Cao and Hegele 2000; Speckman et al 2000). Lamin A/C is sumoylated (Boudreau et al 2012; Zhang and Sarge 2008) and also binds SUMO through a SUMO-interacting motif (SIM) (Moriuchi et al 2016). Lamin A mutations linked to familial partial lipodystrophy alter lamin A sumoylation (Simon et al 2013).…”

Section: 3 Sumo In Familial Partial Lipodystrophymentioning

confidence: 99%

The Roles of SUMO in Metabolic Regulation

Kamynina

2017

SUMO Regulation of Cellular Processes

View full text Add to dashboard Cite

Protein modification with the small ubiquitin-related modifier (SUMO) can affect protein function, enzyme activity, protein-protein interactions, protein stability, protein targeting and cellular localization. SUMO influences the function and regulation of metabolic enzymes within pathways, and in some cases targets entire metabolic pathways by affecting the activity of transcription factors or by facilitating the translocation of entire metabolic pathways to subcellular compartments. SUMO modification is also a key component of nutrient- and metabolic-sensing mechanisms that regulate cellular metabolism. In addition to its established roles in maintaining metabolic homeostasis, there is increasing evidence that SUMO is a key factor in facilitating cellular stress responses through the regulation and/or adaptation of the most fundamental metabolic processes, including energy and nucleotide metabolism. This review focuses on the role of SUMO in cellular metabolism and metabolic disease.

show abstract

Lamin A reassembly at the end of mitosis is regulated by its SUMO-interacting motif

Cited by 25 publications

References 39 publications

K6-linked SUMOylation of BAF regulates nuclear integrity and DNA replication in mammalian cells

K6-linked SUMOylation of BAF regulates nuclear integrity and DNA replication in mammalian cells

Lamins in the nuclear interior − life outside the lamina

The Roles of SUMO in Metabolic Regulation

Contact Info

Product

Resources

About