scholarly journals Man1, an inner nuclear membrane protein, regulates vascular remodeling by modulating transforming growth factor   signaling

Development ◽  
2006 ◽  
Vol 133 (19) ◽  
pp. 3919-3928 ◽  
Author(s):  
A. Ishimura
Keyword(s):  
Growth Factor ◽  
Membrane Protein ◽  
Nuclear Membrane ◽  
Vascular Remodeling ◽  
Transforming Growth Factor ◽  
Growth Factor Signaling ◽  
Inner Nuclear Membrane ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

scholarly journals The Integral Inner Nuclear Membrane Protein MAN1 Physically Interacts with the R-Smad Proteins to Repress Signaling by the Transforming Growth Factor-β Superfamily of Cytokines

2005 ◽  
Vol 280 (16) ◽  
pp. 15992-16001 ◽  
Author(s):  
Deng Pan ◽  
Luis D. Estévez-Salmerón ◽  
Shannon L. Stroschein ◽  
Xueliang Zhu ◽  
Jun He ◽  
...  
Keyword(s):  
Growth Factor ◽  
Membrane Protein ◽  
Nuclear Membrane ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Activin Signaling ◽  
Inner Nuclear Membrane ◽  
Smad Proteins ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

Smad proteins are critical intracellular mediators of the transforming growth factor-β, bone morphogenic proteins (BMPs), and activin signaling. Upon ligand binding, the receptor-associated R-Smads are phosphorylated by the active type I receptor serine/threonine kinases. The phosphorylated R-Smads then form heteromeric complexes with Smad4, translocate into the nucleus, and interact with various transcription factors to regulate the expression of downstream genes. Interaction of Smad proteins with cellular partners in the cytoplasm and nucleus is a critical mechanism by which the activities and expression of the Smad proteins are modulated. Here we report a novel step of regulation of the R-Smad function at the inner nuclear membrane through a physical interaction between the integral inner nuclear membrane protein MAN1 and R-Smads. MAN1, through the RNA recognition motif, associates with R-Smads but not Smad4 at the inner nuclear membrane in a ligand-independent manner. Overexpression of MAN1 results in inhibition of R-Smad phosphorylation, heterodimerization with Smad4 and nuclear translocation, and repression of transcriptional activation of the TGFβ, BMP2, and activin-responsive promoters. This repression of TGFβ, BMP2, and activin signaling is dependent on the MAN1-Smad interaction because a point mutation that disrupts this interaction abolishes the transcriptional repression by MAN1. Thus, MAN1 represents a new class of R-Smad regulators and defines a previously unrecognized regulatory step at the nuclear periphery.

Inner nuclear membrane protein Ima1 is dispensable for intranuclear positioning of centromeres

2011 ◽  
Vol 16 (10) ◽  
pp. 1000-1011 ◽  
Author(s):  
Yasushi Hiraoka ◽  
Hiromi Maekawa ◽  
Haruhiko Asakawa ◽  
Yuji Chikashige ◽  
Tomoko Kojidani ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Nuclear Membrane ◽  
Inner Nuclear Membrane ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

Function and assembly of nuclear pore complex proteins

1999 ◽  
Vol 77 (4) ◽  
pp. 321-329 ◽  
Author(s):  
Khaldon Bodoor ◽  
Sarah Shaikh ◽  
Paul Enarson ◽  
Sharmin Chowdhury ◽  
Davide Salina ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Nuclear Membrane ◽  
Current View ◽  
Nuclear Pore ◽  
Dynamic Component ◽  
Inner Nuclear Membrane ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

Nuclear pore complexes (NPCs) are extremely elaborate structures that mediate the bidirectional movement of macromolecules between the nucleus and cytoplasm. The current view of NPC organization features a massive symmetrical framework that is embedded in the double membranes of the nuclear envelope. It embraces a central channel of as yet ill-defined structure but which may accommodate particles with diameters up to 26 nm provided that they bear specific import/export signals. Attached to both faces of the central framework are peripheral structures, short cytoplasmic filaments, and a nuclear basket assembly, which interact with molecules transiting the NPC. The mechanisms of assembly and the nature of NPC structural intermediates are still poorly understood. However, mutagenesis and expression studies have revealed discrete sequences within certain NPC proteins that are necessary and sufficient for their appropriate targeting. In addition, some details are emerging from observations on cells undergoing mitosis where the nuclear envelope is disassembled and its components, including NPC subunits, are dispersed throughout the mitotic cytoplasm. At the end of mitosis, all of these components are reutilized to form nuclear envelopes in the two daughter cells. To date, it has been possible to define a time course of postmitotic assembly for a group of NPC components (CAN/Nup214, Nup153, POM121, p62 and Tpr) relative to the integral inner nuclear membrane protein LAP2 and the NPC membrane glycoprotein gp210. Nup153, a dynamic component of the nuclear basket, associates with chromatin towards the end of anaphase coincident with, although independent of, the inner nuclear membrane protein, LAP2. Assembly of the remaining proteins follows that of the nuclear membranes and occurs in the sequence POM121, p62, CAN/Nup214 and gp210/Tpr. Since p62 remains as a complex with three other NPC proteins (p58, p54, p45) during mitosis, and CAN/Nup214 maintains a similar interaction with its partner, Nup84, the relative timing of assembly of these additional four proteins may also be inferred. These observations suggest that there is a sequential association of NPC proteins with chromosomes during nuclear envelope reformation and the recruitment of at least eight of these precedes that of gp210. These findings support a model in which it is POM121 rather than gp210 that defines initial membrane-associated NPC assembly intermediates and which may therefore represent an essential component of the central framework of the NPC. Key words: nuclear pore complex, nucleoporin, mitosis, nuclear transport

scholarly journals ESCRT recruitment by the S. cerevisiae inner nuclear membrane protein Heh1 is regulated by Hub1-mediated alternative splicing

2020 ◽  
Vol 133 (24) ◽  
pp. jcs250688 ◽  
Author(s):  
Matías Capella ◽  
Lucía Martín Caballero ◽  
Boris Pfander ◽  
Sigurd Braun ◽  
Stefan Jentsch
Keyword(s):  
Alternative Splicing ◽  
Membrane Protein ◽  
Nuclear Membrane ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Inner Nuclear Membrane ◽  
Growth Defects ◽  
Pore Complexes ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

ABSTRACTMisassembled nuclear pore complexes (NPCs) are removed by sealing off the surrounding nuclear envelope (NE), which is conducted by the endosomal sorting complexes required for transport (ESCRT) machinery. Recruitment of ESCRT proteins to the NE is mediated by the interaction between the ESCRT member Chm7 and the inner nuclear membrane protein Heh1, which belongs to the conserved LEM family. Increased ESCRT recruitment results in excessive membrane scission at damage sites but its regulation remains poorly understood. Here, we show that Hub1-mediated alternative splicing of HEH1 pre-mRNA, resulting in production of its shorter form Heh1-S, is critical for the integrity of the NE in Saccharomyces cerevisiae. ESCRT-III mutants lacking Hub1 or Heh1-S display severe growth defects and accumulate improperly assembled NPCs. This depends on the interaction of Chm7 with the conserved MSC domain, which is only present in the longer variant Heh1-L. Heh1 variants assemble into heterodimers, and we demonstrate that a unique splice segment in Heh1-S suppresses growth defects associated with the uncontrolled interaction between Heh1-L and Chm7. Together, our findings reveal that Hub1-mediated splicing generates Heh1-S to regulate ESCRT recruitment to the NE.This article has an associated First Person interview with the first author of the paper.

scholarly journals MAN1, an Inner Nuclear Membrane Protein That Shares the LEM Domain with Lamina-associated Polypeptide 2 and Emerin

2000 ◽  
Vol 275 (7) ◽  
pp. 4840-4847 ◽  
Author(s):  
Feng Lin ◽  
Deborah L. Blake ◽  
Isabelle Callebaut ◽  
Ilona S. Skerjanc ◽  
Lars Holmer ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Nuclear Membrane ◽  
Inner Nuclear Membrane ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

scholarly journals Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1

EMBO Reports ◽  
2001 ◽  
Vol 2 (10) ◽  
pp. 920-925 ◽  
Author(s):  
Hara Polioudaki ◽  
Niki Kourmouli ◽  
Victoria Drosou ◽  
Alexandra Bakou ◽  
Panayiotis A Theodoropoulos ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Nuclear Membrane ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Inner Nuclear Membrane ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

scholarly journals The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression

2008 ◽  
Vol 182 (5) ◽  
pp. 897-910 ◽  
Author(s):  
Stefanie E. Grund ◽  
Tamás Fischer ◽  
Ghislain G. Cabal ◽  
Oreto Antúnez ◽  
José E. Pérez-Ortín ◽  
...  
Keyword(s):  
Gene Expression ◽  
Membrane Protein ◽  
Nuclear Membrane ◽  
Genetic Interaction ◽  
Nuclear Pore ◽  
Inner Nuclear Membrane ◽  
Regulated Gene Expression ◽  
Inner Nuclear Membrane Protein ◽  
Subtelomeric Regions ◽  
Nuclear Membrane Protein

Inner nuclear membrane proteins containing a LEM (LAP2, emerin, and MAN1) domain participate in different processes, including chromatin organization, gene expression, and nuclear envelope biogenesis. In this study, we identify a robust genetic interaction between transcription export (TREX) factors and yeast Src1, an integral inner nuclear membrane protein that is homologous to vertebrate LEM2. DNA macroarray analysis revealed that the expression of the phosphate-regulated genes PHO11, PHO12, and PHO84 is up-regulated in src1Δ cells. Notably, these PHO genes are located in subtelomeric regions of chromatin and exhibit a perinuclear location in vivo. Src1 spans the nuclear membrane twice and exposes its N and C domains with putative DNA-binding motifs to the nucleoplasm. Genome-wide chromatin immunoprecipitation–on-chip analyses indicated that Src1 is highly enriched at telomeres and subtelomeric regions of the yeast chromosomes. Our data show that the inner nuclear membrane protein Src1 functions at the interface between subtelomeric gene expression and TREX-dependent messenger RNA export through the nuclear pore complexes.

scholarly journals A transmembrane inner nuclear membrane protein in the mitotic spindle

Nucleus ◽  
2010 ◽  
Vol 1 (3) ◽  
pp. 249-253 ◽  
Author(s):  
Ricardo Figueroa ◽  
Santhosh Gudise ◽  
Veronica Larsson ◽  
Einar Hallberg
Keyword(s):  
Membrane Protein ◽  
Nuclear Membrane ◽  
Mitotic Spindle ◽  
Inner Nuclear Membrane ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein
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