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2000 1
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2014 5
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2017 5
2018 8
2019 3
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An improved smaller biotin ligase for BioID proximity labeling
Kim DI, et al. Mol Biol Cell 2016. PMID 26912792 Free PMC article.
The BioID method uses a promiscuous biotin ligase to detect protein-protein associations as well as proximate proteins in living cells. ...BioID2 enables more-selective targeting of fusion proteins, requires less biotin supplementation, and exhibits enhanced labeling of proximate proteins. ...
The BioID method uses a promiscuous biotin ligase to detect protein-protein associations as well as proximate proteins
SUN2 Overexpression Deforms Nuclear Shape and Inhibits HIV.
Donahue DA, et al. J Virol 2016. PMID 26865710 Free PMC article.
SUN2 is an inner nuclear membrane protein belonging to the linker of nucleoskeleton and cytoskeleton complex. We have analyzed here the role of SUN2 in HIV infection. ...We show that SUN2 overexpression blocks the infection of certain strains of HIV before nuclear entry. Mutation of the viral capsid protein yielded SUN2-resistant HIV. ...
SUN2 is an inner nuclear membrane protein belonging to the linker of nucleoskeleton and cytoskeleton complex. We have analyzed
SUN2 Modulates HIV-1 Infection and Latency through Association with Lamin A/C To Maintain the Repressive Chromatin.
Sun WW, et al. mBio 2018. PMID 29717016 Free PMC article.
Here we revealed that "Sad1 and UNC84 domain containing 2" (SUN2), an inner nuclear membrane protein, maintained the repressive chromatin and inhibited HIV LTR-driven transcription of proviral DNA through an association with lamin A/C. ...In this study, we performed in-depth virological and cell biological studies and discovered that an inner nuclear membrane protein, SUN2, is a novel chromatin reassembly factor that maintains repressive chromatin and thus modulates HIV-1 transcription and latency: therefore, targeting SUN2 may lead to new strategies for HIV cure....
Here we revealed that "Sad1 and UNC84 domain containing 2" (SUN2), an inner nuclear membrane protein, maintained the repressiv …
SUN2 Silencing Impairs CD4 T Cell Proliferation and Alters Sensitivity to HIV-1 Infection Independently of Cyclophilin A.
Donahue DA, et al. J Virol 2017. PMID 28077629 Free PMC article.
We previously reported that the overexpression of SUN2, an inner nuclear membrane protein and LINC complex component, inhibits HIV infection between the steps of reverse transcription and nuclear import in a capsid-specific manner. ...We previously reported that the overexpression of the LINC complex protein SUN2 inhibits HIV infection by targeting the viral capsid and blocking infection before the virus enters the nucleus. ...
We previously reported that the overexpression of SUN2, an inner nuclear membrane protein and LINC complex component, inhibits …
A molecular model for LINC complex regulation: activation of SUN2 for KASH binding.
Jahed Z, et al. Mol Biol Cell 2018. PMID 29995584 Free PMC article.
Two major components of these complexes are members of the SUN and KASH protein families that interact in the perinuclear space to allow the transmission of mechanochemical signals across the NE. Structural details of the mammalian SUN domain protein SUN2 have established that SUN2 must form a trimer to bind to KASH, and that this trimerization is mediated through two predicted coiled-coil regions of the protein, CC1 and CC2, which precede the SUN domain. ...
Two major components of these complexes are members of the SUN and KASH protein families that interact in the perinuclear space to al …
Let me in: Control of HIV nuclear entry at the nuclear envelope
Bhargava A, et al. Cytokine Growth Factor Rev 2018 - Review. PMID 29526438
Here, we review the viral and host factors that favor or inhibit HIV entry into the nucleus, including the viral capsid, integrase, the central viral DNA flap, and the host proteins CPSF6, TNPO3, Nucleoporins, SUN1, SUN2, Cyclophilin A and MX2. ...
Here, we review the viral and host factors that favor or inhibit HIV entry into the nucleus, including the viral capsid, integrase, the cent …
SUN2 exerts tumor suppressor functions by suppressing the Warburg effect in lung cancer.
Lv XB, et al. Sci Rep 2015. PMID 26658802 Free PMC article.
We found that SUN2 expression was decreased in lung cancer tissue compared with paired normal tissues and that higher SUN2 levels predicted better overall survival and first progression survival. Overexpression of SUN2 inhibits cell proliferation, colony formation and migration in lung cancer, whereas knockdown of SUN2 promotes cell proliferation and migration. ...
We found that SUN2 expression was decreased in lung cancer tissue compared with paired normal tissues and that higher SUN2 lev …
Effects of Inner Nuclear Membrane Proteins SUN1/UNC-84A and SUN2/UNC-84B on the Early Steps of HIV-1 Infection.
Schaller T, et al. J Virol 2017. PMID 28747499 Free PMC article.
To identify host proteins that may contribute to these processes, we performed an overexpression screen of known membrane-associated NE proteins. ...While overexpression of these proteins reduces HIV-1 infection, disruption of the individual SUN2 and SUN1 genes leads to a mild reduction or no effect on infectivity, respectively. ...
To identify host proteins that may contribute to these processes, we performed an overexpression screen of known membrane-associated …
Molecular Insights into the Mechanisms of SUN1 Oligomerization in the Nuclear Envelope
Jahed Z, et al. Biophys J 2018. PMID 29539404 Free PMC article.
The LINC complex is found in a wide variety of organisms and is formed by the transluminal interaction between outer- and inner-nuclear-membrane KASH and SUN proteins, respectively. Most extensively studied are SUN1 and SUN2 proteins, which are widely expressed in mammals. Although SUN1 and SUN2 play functionally redundant roles in several cellular processes, more recent studies have revealed diverse and distinct functions for SUN1. ...
The LINC complex is found in a wide variety of organisms and is formed by the transluminal interaction between outer- and inner-nuclear-memb …
A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane.
Turgay Y, et al. EMBO J 2010. PMID 20551905 Free PMC article.
Unexpectedly, also the C-terminal, lumenal SUN domain of SUN2 supports NE localization, showing that targeting elements are not limited to cytoplasmic or transmembrane domains of INM proteins. Together, SUN2 represents the first mammalian INM protein relying on a functional cNLS, a Golgi retrieval signal and a perinuclear domain to mediate targeting to the INM....
Unexpectedly, also the C-terminal, lumenal SUN domain of SUN2 supports NE localization, showing that targeting elements are not limit …
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