Destination: inner nuclear membrane

Katta, Santharam S.; Smoyer, Christine J.; Jaspersen, Sue L.

doi:10.1016/j.tcb.2013.10.006

Cited by 105 publications

(113 citation statements)

References 87 publications

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“…S1E). These data indicate that, as previously documented for several inner nuclear membrane proteins (Katta et al, 2014;Laba et al, 2014), redundant mechanisms and/or signals are required for proper NPC targeting of Pom33. In the future, additional studies will be required to understand how the two new Pom33 features described in this study cooperate with other factors to ensure proper NPC assembly and function.…”

Section: Discussionsupporting

confidence: 82%

“…Although the precise mechanisms ensuring proper pore membrane targeting have only been defined for a few Poms, it appears that, as for integral proteins of the INM (reviewed in Katta et al, 2014, Laba et al, 2014, multiple distinct determinants contribute to this process. For instance, the transmembrane domain of vertebrate gp210 has been shown to be sufficient for NPC targeting, but its short C-terminal cytoplasmic tail encompasses an additional sorting determinant (Wozniak and Blobel, 1992).…”

Section: Introductionmentioning

confidence: 99%

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Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding

Floch

Tareste

Fuchs

et al. 2014

Journal of Cell Science

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Pom33 is an integral membrane protein of the yeast nuclear pore complex (NPC), required for proper NPC distribution and assembly. To characterize Pom33 NPC-targeting determinants, we performed immunoprecipitation experiments followed by mass spectrometry analyses. This identified a novel Pom33 partner, the nuclear import factor Kap123. In vitro experiments revealed a direct interaction between Pom33 C-terminal domain (CTD) and Kap123. In silico analysis predicted the presence of two amphipathic α-helices within Pom33-CTD. Circular dichroism and liposome co-flotation assays showed that this domain is able to fold into α-helices in the presence of liposomes and preferentially binds to highly curved lipid membranes. When expressed in yeast, under conditions abolishing Pom33-CTD membrane association, this domain behaves as a Kap123-dependent nuclear localization signal (NLS). While deletion of Pom33 C-terminal domain (Pom33ΔCTD-GFP) impairs Pom33 stability and NPC targeting, mutants affecting either Kap123 binding or the amphipathic properties of the α-helices do not display any detectable defect. However, combined impairment of lipid and Kap123 binding affects Pom33 targeting to NPCs. These data highlight the requirement of multiple determinants and mechanisms for proper NPC localization of Pom33.

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Section: Discussionsupporting

confidence: 82%

Section: Introductionmentioning

confidence: 99%

Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding

Floch

Tareste

Fuchs

et al. 2014

Journal of Cell Science

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“…Most prominently, a diffusion-retention model has been proposed for many INM proteins (e.g. lamin B receptor (LBR)) (20,21). This model suggests that proteins synthesized in the ER rapidly diffuse laterally in the ONM, pass through peripheral channels existing between the nuclear pore complex and the pore membrane, and then become tethered in the INM via nucleoplasmic interactions with nuclear lamins or chromatin (22)(23)(24).…”

Section: Edited By Roger J Colbranmentioning

confidence: 99%

“…Because the peripheral channels are thought to be about 10 nm, nucleoplasmic domains cannot exceed masses of Ͼ60 kDa (25)(26)(27). Although the exact signals are unknown, at least 15 proteins have been shown to translocate through peripheral channels to reside on the INM (20,21,28). Current findings show that a wide range of mechanisms underlie transmembrane INM transport, including use of phenylalanine-glycine (FG) motifs, use of nucleoporins, and use of the peripheral channels or the central channel or both (20,21).…”

Section: Edited By Roger J Colbranmentioning

confidence: 99%

Sequences within the C Terminus of the Metabotropic Glutamate Receptor 5 (mGluR5) Are Responsible for Inner Nuclear Membrane Localization

Jong¹,

Harmon

Kumar

et al. 2017

Journal of Biological Chemistry

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Edited by Roger J. ColbranTraditionally, G-protein-coupled receptors (GPCR) are thought to be located on the cell surface where they transmit extracellular signals to the cytoplasm. However, recent studies indicate that some GPCRs are also localized to various subcellular compartments such as the nucleus where they appear required for various biological functions. For example, the metabotropic glutamate receptor 5 (mGluR5) is concentrated at the inner nuclear membrane (INM) where it mediates Ca 2؉ changes in the nucleoplasm by coupling with G q/11 . Here, we identified a region within the C-terminal domain (amino acids 852-876) that is necessary and sufficient for INM localization of the receptor. Because these sequences do not correspond to known nuclear localization signal motifs, they represent a new motif for INM trafficking. mGluR5 is also trafficked to the plasma membrane where it undergoes re-cycling/degradation in a separate receptor pool, one that does not interact with the nuclear mGluR5 pool. Finally, our data suggest that once at the INM, mGluR5 is stably retained via interactions with chromatin. Thus, mGluR5 is perfectly positioned to regulate nucleoplasmic Ca 2؉ in situ.From their position on the cell surface, G-protein-coupled receptors (GPCRs) 3 can transform external stimuli into a broad range of signaling pathways within the cell. A mounting body of evidence indicates that many GPCRs are also localized inside the cell where they may couple to different signaling systems, display unique desensitization patterns, and/or exhibit distinct patterns of subcellular distribution (1-5). For example, GPCRs have been found on mitochondria (6), endoplasmic reticulum (ER) membranes (7), lysosomes (8, 9), and on nuclear membranes (10 -12). Certain GPCRs are even found within the nucleoplasm on nuclear bodies and/or nuclear invaginations (13-16). Although many intracellular GPCRs are activated at the cell surface and subsequently trafficked to their intracellular site, others can be activated at their subcellular location via so-called intracrine ligands that can enter cells via diffusion or be made in situ, endocytosed, and/or transported through channels or pores (12,17,18). Intracellular GPCRs can also function independently governing processes such as synaptic plasticity (19), myocyte contraction (15), and angiogenesis (16). Collectively, the present findings reinforce the notion that intracellular GPCRs play a dynamic role in generating and shaping intracellular signaling pathways.As many GPCRs are on or in the nucleus, the question arises as to how they get there. Various possibilities exist to transfer membrane proteins from the outer to the inner nuclear membrane (ONM and INM), including vesicle fusion, membrane rupture, and channel-mediated pathways. Most prominently, a diffusion-retention model has been proposed for many INM proteins (e.g. lamin B receptor (LBR)) (20,21). This model suggests that proteins synthesized in the ER rapidly diffuse laterally in the ONM, pass through peripheral channels ex...

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“…Specifically, the luminal domains of SUN proteins must overcome the POM layer within NPCs (see Box 1). One hypothesis is the existence of ∼10-nm peripheral channels within each spoke of the NPC through which INM proteins could be transported (Maimon et al, 2012;Katta et al, 2014). Conversely, a more recent structural The nuclear envelope narrows at sites of nuclear envelope expansion; here, the interaction of SUN1 with nucleoporin Pom121 helps to narrow the nuclear envelope and so promotes de novo NPC assembly.…”

Section: Trafficking Of Sun Proteins Across the Npc For Inm Localizationmentioning

confidence: 99%

The LINC and NPC relationship – it's complicated!

Jahed

Soheilypour

Peyro

et al. 2016

Journal of Cell Science

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The genetic information of eukaryotic cells is enclosed within a double-layered nuclear envelope, which comprises an inner and outer nuclear membrane. Several transmembrane proteins locate to the nuclear envelope; however, only two integral protein complexes span the nuclear envelope and connect the inside of the nucleus to the cytoplasm. The nuclear pore complex (NPC) acts as a gateway for molecular exchange between the interior of the nucleus and the cytoplasm, whereas so-called LINC complexes physically link the nucleoskeleton and the cytoskeleton. In this Commentary, we will discuss recent studies that have established direct functional associations between these two complexes. The assembly of NPCs and their even distribution throughout the nuclear envelope is dependent on components of the LINC complex. Additionally, LINC complex formation is dependent on the successful localization of inner nuclear membrane components of LINC complexes and their transport through the NPC. Furthermore, the architecture of the nuclear envelope depends on both protein complexes. Finally, we will present recent evidence showing that LINC complexes can affect nucleo-cytoplasmic transport through the NPC, further highlighting the importance of understanding the associations of these essential complexes at the nuclear envelope.

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Destination: inner nuclear membrane

Cited by 105 publications

References 87 publications

Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding

Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding

Sequences within the C Terminus of the Metabotropic Glutamate Receptor 5 (mGluR5) Are Responsible for Inner Nuclear Membrane Localization

The LINC and NPC relationship – it's complicated!

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