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179 results on '"Lim, Roderick Y. H."'

7. Dynamic molecular mechanism of the nuclear pore complex permeability barrier

Author

Kozai, Toshiya, primary, Fernandez-Martinez, Javier, additional, van Eeuwen, Trevor, additional, Gallardo, Paola, additional, Kapinos, Larisa E., additional, Mazur, Adam, additional, Zhang, Wenzhu, additional, Tempkin, Jeremy, additional, Panatala, Radhakrishnan, additional, Delgado-Izquierdo, Maria, additional, Raveh, Barak, additional, Sali, Andrej, additional, Chait, Brian T., additional, Veenhoff, Liesbeth M., additional, Rout, Michael P., additional, and Lim, Roderick Y. H., additional

Published
2023
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11. Karyopherin compensation fortifies the nuclear pore complex against nucleocytoplasmic leakage

Author

Kalita, Joanna, Kapinos, Larisa E., Tiantian Zheng, Rencurel, Chantal, Zilman, Anton, and Lim, Roderick Y. H.

Subjects
Nuclear pore complex, stomatognathic diseases, FG Nucleoporins, Nucleocytoplasmic transport, Nuclear transport receptors, otorhinolaryngologic diseases, Karyopherins
Abstract

Nuclear pore complexes (NPCs) discriminate non-specific macromolecules from importin and exportin receptors, collectively termed karyopherins (Kaps), that mediate nucleocytoplasmic transport. This selective barrier function is attributed to the behavior of intrinsically disordered phenylalanine-glycine nucleoporins (FG Nups) that guard the NPC channel. However, NPCs in vivo are typically enriched with different Kaps, and how they impact on the NPC barrier remains unknown. Here, we show that two major Kaps, importinβ1/karyopherinβ1 (Kapβ1) and exportin 1/chromosomal maintenance 1 (CRM1) are required to fortify NPC barrier function in vivo. Their enrichment at the NPC is sustained by promiscuous binding interactions with the FG Nups resulting in a compensatory mechanism that is constrained by their respective cellular abundances and different binding kinetics as evidenced for another Kap, Importin-5. Hence, Kapβ1 and CRM1 are engaged in the reinforcement of the NPC barrier function. Consequently, we find that NPC malfunctionand nucleocytoplasmic leakage result from poor Kap enrichment.

Published
2022
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27. Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria

Author

Carlos Santos, José, Boucher, Dave, Schneider, Larisa Kapinos, Demarco, Benjamin, Dilucca, Marisa, Shkarina, Kateryna, Heilig, Rosalie, Chen, Kaiwen W., Lim, Roderick Y. H., and Broz, Petr

Abstract

The human non-canonical inflammasome controls caspase-4 activation and gasdermin-Ddependent pyroptosis in response to cytosolic bacterial lipopolysaccharide (LPS). Since LPS binds and oligomerizes caspase-4, the pathway is thought to proceed without dedicated LPS sensors or an activation platform. Here we report that interferon-induced guanylate-binding proteins (GBPs) are required for non-canonical inflammasome activation by cytosolic Salmonella or upon cytosolic delivery of LPS. GBP1 associates with the surface of cytosolic Salmonella seconds after bacterial escape from their vacuole, initiating the recruitment of GBP2-4 to assemble a GBP coat. The GBP coat then promotes the recruitment of caspase-4 to the bacterial surface and caspase activation, in absence of bacteriolysis. Mechanistically, GBP1 binds LPS with high affinity through electrostatic interactions. Our findings indicate that in human epithelial cells GBP1 acts as a cytosolic LPS sensor and assembles a platform for caspase-4 recruitment and activation at LPS-containing membranes as the first step of noncanonical inflammasome signaling. [ABSTRACT FROM AUTHOR]

Published
2020
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28. Karyopherin enrichment at the nuclear pore complex attenuates Ran permeability.

Author

Barbato, Suncica, Kapinos, Larisa E., Rencurel, Chantal, and Lim, Roderick Y. H.

Subjects
NUCLEAR transport, PERMEABILITY, GUANOSINE triphosphate, NUCLEAR membranes, SMALL molecules, CYTOPLASM
Abstract

Ran is a small GTPase whose nucleotide-bound forms cycle through nuclear pore complexes (NPCs) to direct nucleocytoplasmic transport (NCT). Generally, Ran guanosine triphosphate (RanGTP) binds cargocarrying karyopherin receptors (Kaps) in the nucleus and releases them into the cytoplasm following hydrolysis to Ran guanosine diphosphate (RanGDP). This generates a remarkably steep Ran gradient across the nuclear envelope that sustains compartment-specific cargo delivery and accumulation. However, because NPCs are permeable to small molecules of comparable size, it is unclear how an uncontrolled mixing of RanGTP and RanGDP is prevented. Here, we find that an NPCenriched pool of karyopherin subunit beta 1 (KPNB1, hereafter referred to as Kapß1) selectively mediates Ran diffusion across the pore but not passive molecules of similar size (e.g. GFP). This is due to RanGTP having a stronger binding interaction with Kapß1 than RanGDP. For this reason, the RanGDP importer, nuclear transport factor 2, facilitates the return of RanGDP into the nucleus following GTP hydrolysis. Accordingly, the enrichment of Kapß1 at NPCs may function as a retention mechanism that preserves the sharp transition of RanGTP and RanGDP in the nucleus and cytoplasm, respectively. [ABSTRACT FROM AUTHOR]

Published
2020
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31. Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimerrs Disease

Author

Eftekharzadeh, Bahareh, primary, Daigle, J. Gavin, additional, Kapinos, Larisa E., additional, Dujardin, Simon, additional, Coyne, Alyssa, additional, Miller, Sean J., additional, Cook, Casey, additional, Grima, Jonathan C., additional, Bennett, Rachel E., additional, Schiantarelli, Julia, additional, Carlomagno, Yari, additional, Tepper, Katharina, additional, Amaral, Ana C., additional, DeVos, Sarah L., additional, Vanderburgh, Charles R., additional, Maesako, Masato, additional, Commins, Caitlin, additional, Corjuc, Bianca T., additional, Gonzalez, Jose Antonio, additional, Mertens, Jerome, additional, Mackenzie, Danny, additional, Vidensky, Svetlana, additional, Valle, Nicholas J., additional, Hussain, Uzma, additional, Gage, Fred H., additional, Troncoso, Juan, additional, Salvatella, Xavier, additional, Lim, Roderick Y. H., additional, Mandelkow, Eckhard, additional, Wegmann, Susanne, additional, Petrucelli, Leonard, additional, Rothstein, Jeffrey D., additional, and Hyman, Bradley T., additional

Published
2018
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36. Structural centrosome aberrations promote non‐cell‐autonomous invasiveness.

Author

Ganier, Olivier, Schnerch, Dominik, Oertle, Philipp, Lim, Roderick Y. H., Plodinec, Marija, and Nigg, Erich A.

Subjects
CENTROSOMES, CHROMOSOME abnormalities, MITOSIS, CYTOSKELETON, CADHERINS
Abstract

Abstract: Centrosomes are the main microtubule‐organizing centers of animal cells. Although centrosome aberrations are common in tumors, their consequences remain subject to debate. Here, we studied the impact of structural centrosome aberrations, induced by deregulated expression of ninein‐like protein (NLP), on epithelial spheres grown in Matrigel matrices. We demonstrate that NLP‐induced structural centrosome aberrations trigger the escape (“budding”) of living cells from epithelia. Remarkably, all cells disseminating into the matrix were undergoing mitosis. This invasive behavior reflects a novel mechanism that depends on the acquisition of two distinct properties. First, NLP‐induced centrosome aberrations trigger a re‐organization of the cytoskeleton, which stabilizes microtubules and weakens E‐cadherin junctions during mitosis. Second, atomic force microscopy reveals that cells harboring these centrosome aberrations display increased stiffness. As a consequence, mitotic cells are pushed out of mosaic epithelia, particularly if they lack centrosome aberrations. We conclude that centrosome aberrations can trigger cell dissemination through a novel, non‐cell‐autonomous mechanism, raising the prospect that centrosome aberrations contribute to the dissemination of metastatic cells harboring normal centrosomes. [ABSTRACT FROM AUTHOR]

Published
2018
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39. Correction to Disordered Proteinaceous Machines

Author

Fuxreiter, Monika, primary, Tóth-Petróczy, Ágnes, additional, Kraut, Daniel A., additional, Matouschek, Andreas, additional, Lim, Roderick Y. H., additional, Xue, Bin, additional, Kurgan, Lukasz, additional, and Uversky, Vladimir N., additional

Published
2015
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41. Disordered Proteinaceous Machines

Author

Fuxreiter, Monika, primary, Tóth-Petróczy, Ágnes, additional, Kraut, Daniel A., additional, Matouschek, Andreas T., additional, Lim, Roderick Y. H., additional, Xue, Bin, additional, Kurgan, Lukasz, additional, and Uversky, Vladimir N., additional

Published
2014
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44. The nanomechanical signature of breast cancer

Author

Plodinec, Marija, primary, Loparic, Marko, additional, Monnier, Christophe A., additional, Obermann, Ellen C., additional, Zanetti-Dallenbach, Rosanna, additional, Oertle, Philipp, additional, Hyotyla, Janne T., additional, Aebi, Ueli, additional, Bentires-Alj, Mohamed, additional, Lim, Roderick Y. H., additional, and Schoenenberger, Cora-Ann, additional

Published
2012
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