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LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/jsbi.1996.0013openalex-snapshot
Computer Visualization of Three-Dimensional Image Data Using IMOD
inferredcites →https://doi.org/10.1016/j.ceb.2008.09.010openalex-snapshot
Reorganization of the nuclear envelope during open mitosis
inferredcites →https://doi.org/10.1016/j.ceb.2015.03.005openalex-snapshot
Networking in the nucleus: a spotlight on LEM-domain proteins
inferredcites →https://doi.org/10.1016/j.ceb.2016.03.008openalex-snapshot
Novel ESCRT functions in cell biology: spiraling out of control?
inferredcites →https://doi.org/10.1016/j.cell.2012.04.028openalex-snapshot
Functional Repurposing Revealed by Comparing S. pombe and S. cerevisiae Genetic Interactions
inferredcites →https://doi.org/10.1016/j.cell.2012.04.043openalex-snapshot
Coordination of Kinase and Phosphatase Activities by Lem4 Enables Nuclear Envelope Reassembly during Mitosis
inferredcites →https://doi.org/10.1016/j.cell.2013.10.003openalex-snapshot
The Frustrated Gene: Origins of Eukaryotic Gene Expression
inferredcites →https://doi.org/10.1016/j.cell.2014.09.012openalex-snapshot
Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4
inferredcites →https://doi.org/10.1016/j.cub.2016.07.039openalex-snapshot
Membrane Binding by CHMP7 Coordinates ESCRT-III-Dependent Nuclear Envelope Reformation
inferredcites →https://doi.org/10.1016/j.febslet.2006.10.060openalex-snapshot
The inner nuclear membrane protein Lem2 is critical for normal nuclear envelope morphology
inferredcites →https://doi.org/10.1016/j.jmb.2015.11.004openalex-snapshot
Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines
inferredcites →https://doi.org/10.1016/j.jsb.2005.07.007openalex-snapshot
Automated electron microscope tomography using robust prediction of specimen movements
inferredcites →https://doi.org/10.1016/j.jsb.2005.12.009openalex-snapshot
Tilt-series and electron microscope alignment for the correction of the non-perpendicularity of beam and tilt-axis
inferredcites →https://doi.org/10.1016/s0074-7696(08)60069-8openalex-snapshot
The Evolution of the Mitotic Spindle
inferredcites →https://doi.org/10.1016/s0074-7696(08)60235-1openalex-snapshot
Variant Mitoses in Lower Eukaryotes: Indicators of the Evolution of Mitosis?
inferredcites →https://doi.org/10.1016/s0092-8674(03)00714-1openalex-snapshot
The Protein Network of HIV Budding
inferredcites →https://doi.org/10.1016/s0962-8924(00)01798-0openalex-snapshot
Spindle pole body duplication: a model for centrosome duplication?
inferredcites →https://doi.org/10.1038/nature05075openalex-snapshot
Karyopherin-mediated import of integral inner nuclear membrane proteins
inferredcites →https://doi.org/10.1038/nature14408openalex-snapshot
Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing
inferredcites →https://doi.org/10.1038/nature14503openalex-snapshot
ESCRT-III controls nuclear envelope reformation
inferredcites →https://doi.org/10.1038/ncb1163openalex-snapshot
Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery
inferredcites →https://doi.org/10.1038/nsmb.1512openalex-snapshot
Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B
inferredcites →https://doi.org/10.1073/pnas.1005938107openalex-snapshot
Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance
inferredcites →https://doi.org/10.1074/jbc.m116.743211openalex-snapshot
Role of Inner Nuclear Membrane Protein Complex Lem2-Nur1 in Heterochromatic Gene Silencing
inferredcites →https://doi.org/10.1083/jcb.200504140openalex-snapshot
The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
inferredcites →https://doi.org/10.1083/jcb.200812108openalex-snapshot
The S. pombe mitotic regulator Cut12 promotes spindle pole body activation and integration into the nuclear envelope
inferredcites →https://doi.org/10.1083/jcb.200901106openalex-snapshot
Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo
inferredcites →https://doi.org/10.1083/jcb.201012154openalex-snapshot
POM121 and Sun1 play a role in early steps of interphase NPC assembly
inferredcites →https://doi.org/10.1083/jcb.201106076openalex-snapshot
Brr6 drives the Schizosaccharomyces pombe spindle pole body nuclear envelope insertion/extrusion cycle
inferredcites →https://doi.org/10.1091/mbc.10.7.2393openalex-snapshot
Saccharomyces cerevisiae MPS2Encodes a Membrane Protein Localized at the Spindle Pole Body and the Nuclear Envelope
inferredcites →https://doi.org/10.1091/mbc.8.8.1461openalex-snapshot
The spindle pole body of Schizosaccharomyces pombe enters and leaves the nuclear envelope as the cell cycle proceeds.
inferredcites →https://doi.org/10.1091/mbc.e08-05-0475openalex-snapshot
Biochemical Analyses of Human IST1 and Its Function in Cytokinesis
inferredcites →https://doi.org/10.1091/mbc.e08-08-0883openalex-snapshot
The Nucleoporin Nup153 Has Separable Roles in Both Early Mitotic Progression and the Resolution of Mitosis
inferredcites →https://doi.org/10.1093/nar/gkv1058openalex-snapshot
Inner nuclear envelope protein SUN1 plays a prominent role in mammalian mRNA export
inferredcites →https://doi.org/10.1101/gad.271288.115openalex-snapshot
Control of heterochromatin localization and silencing by the nuclear membrane protein Lem2
inferredcites →https://doi.org/10.1111/gtc.12385openalex-snapshot
Inner nuclear membrane protein Lem2 augments heterochromatin formation in response to nutritional conditions
inferredcites →https://doi.org/10.1111/j.1365-2818.2008.01977.xopenalex-snapshot
Correction for non‐perpendicularity of beam and tilt axis in tomographic reconstructions with the IMOD package
inferredcites →https://doi.org/10.1111/j.1600-0854.2008.00847.xopenalex-snapshot
Spastin Couples Microtubule Severing to Membrane Traffic in Completion of Cytokinesis and Secretion
inferredcites →https://doi.org/10.1126/science.1180823openalex-snapshot
The Genetic Landscape of a Cell
inferredcites →https://doi.org/10.1126/science.aad7297openalex-snapshot
Nuclear envelope rupture and repair during cancer cell migration
inferredcites →https://doi.org/10.1126/science.aad7611openalex-snapshot
ESCRT III repairs nuclear envelope ruptures during cell migration to limit DNA damage and cell death
inferredcites →https://doi.org/10.1126/science.aad8305openalex-snapshot
Structure and membrane remodeling activity of ESCRT-III helical polymers
inferredcites →https://doi.org/10.1128/jb.124.1.511-523.1975openalex-snapshot
Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1128/mcb.00270-09openalex-snapshot
Overlapping Functions of Nuclear Envelope Proteins NET25 (Lem2) and Emerin in Regulation of Extracellular Signal-Regulated Kinase Signaling in Myoblast Differentiation
inferredcites →https://doi.org/10.1146/annurev-biochem-072909-101058openalex-snapshot
Membrane Fission Reactions of the Mammalian ESCRT Pathway
inferredcites →https://doi.org/10.1146/annurev.cellbio.20.022003.114106openalex-snapshot
THE BUDDING YEAST SPINDLE POLE BODY: Structure, Duplication, and Function
inferredcites →https://doi.org/10.1242/jcs.02701openalex-snapshot
LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins
inferredcites →https://doi.org/10.1242/jcs.9.2.475openalex-snapshot
Mitosis in the fission yeast Schizosaccharomyces pombe: a comparative study with light and electron microscopy
inferredcites →https://doi.org/10.1371/journal.pone.0116196openalex-snapshot
Nuclear Envelope Protein Lem2 is Required for Mouse Development and Regulates MAP and AKT Kinases
inferredcites →https://doi.org/10.1371/journal.pone.0132489openalex-snapshot
The Inner Nuclear Membrane Protein Src1 Is Required for Stable Post-Mitotic Progression into G1 in Aspergillus nidulans
inferredcites →https://doi.org/10.15252/embj.201694574openalex-snapshot
Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing
inferredcites →https://doi.org/10.1534/genetics.110.119149openalex-snapshot
Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1534/genetics.115.178939openalex-snapshot
Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7
inferredcites →https://doi.org/10.2144/000112226openalex-snapshot
High-Pressure Freezing, Cellular Tomography, and Structural Cell Biology
inferredcites →https://doi.org/10.2144/000113909openalex-snapshot
Attenuated protein expression vectors for use in siRNA rescue experiments
inferredcites →https://doi.org/10.4161/nucl.18824openalex-snapshot
Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1016/j.cub.2016.07.039openalex-snapshot
Membrane Binding by CHMP7 Coordinates ESCRT-III-Dependent Nuclear Envelope Reformation
inferred← citeshttps://doi.org/10.1083/jcb.201910119openalex-snapshot
Cdc42 GTPase regulates ESCRTs in nuclear envelope sealing and ER remodeling
inferred← citeshttps://doi.org/10.1101/476630openalex-snapshot
ESCRT-III accumulates in micronuclei with ruptured nuclear envelopes
inferred← citeshttps://doi.org/10.15252/embj.201694574openalex-snapshot
Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing
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