Search Results - "Port, Sarah A."

Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association by Jiao, Junyi, He, Mengze, Port, Sarah A, Baker, Richard W, Xu, Yonggang, Qu, Hong, Xiong, Yujian, Wang, Yukun, Jin, Huaizhou, Eisemann, Travis J, Hughson, Frederick M, Zhang, Yongli

“…Sec1/Munc18-family (SM) proteins are required for SNARE-mediated membrane fusion, but their mechanism(s) of action remain controversial. Using single-molecule…”
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Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export by Port, Sarah A., Monecke, Thomas, Dickmanns, Achim, Spillner, Christiane, Hofele, Romina, Urlaub, Henning, Ficner, Ralf, Kehlenbach, Ralph H.

“…CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine…”
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Auxin efflux by PIN-FORMED proteins is activated by two different protein kinases, D6 PROTEIN KINASE and PINOID by Zourelidou, Melina, Absmanner, Birgit, Weller, Benjamin, Barbosa, Inês C R, Willige, Björn C, Fastner, Astrid, Streit, Verena, Port, Sarah A, Colcombet, Jean, de la Fuente van Bentem, Sergio, Hirt, Heribert, Kuster, Bernhard, Schulze, Waltraud X, Hammes, Ulrich Z, Schwechheimer, Claus

“…The development and morphology of vascular plants is critically determined by synthesis and proper distribution of the phytohormone auxin. The directed…”
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The structural basis of Rubisco phase separation in the pyrenoid by He, Shan, Chou, Hui-Ting, Matthies, Doreen, Wunder, Tobias, Meyer, Moritz T., Atkinson, Nicky, Martinez-Sanchez, Antonio, Jeffrey, Philip D., Port, Sarah A., Patena, Weronika, He, Guanhua, Chen, Vivian K., Hughson, Frederick M., McCormick, Alistair J., Mueller-Cajar, Oliver, Engel, Benjamin D., Yu, Zhiheng, Jonikas, Martin C.

“…Approximately one-third of global CO 2 fixation occurs in a phase-separated algal organelle called the pyrenoid. The existing data suggest that the pyrenoid…”
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The Oncogenic Fusion Proteins SET-Nup214 and Sequestosome-1 (SQSTM1)-Nup214 Form Dynamic Nuclear Bodies and Differentially Affect Nuclear Protein and Poly(A)+ RNA Export by Port, Sarah A., Mendes, Adélia, Valkova, Christina, Spillner, Christiane, Fahrenkrog, Birthe, Kaether, Christoph, Kehlenbach, Ralph H.

“…Genetic rearrangements are a hallmark of several forms of leukemia and can lead to oncogenic fusion proteins. One example of an affected chromosomal region is…”
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The SQSTM1-NUP214 fusion protein interacts with Crm1, activates Hoxa and Meis1 genes, and drives leukemogenesis in mice by Lavau, Catherine P, Aumann, Waitman K, Sze, Sei-Gyung K, Gupta, Veerain, Ripple, Katelyn, Port, Sarah A, Kehlenbach, Ralph H, Wechsler, Daniel S

“…The NUP98 and NUP214 nucleoporins (NUPs) are recurrently fused to heterologous proteins in leukemia. The resulting chimeric oncoproteins retain the…”
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A nuclear export sequence promotes CRM1-dependent targeting of the nucleoporin Nup214 to the nuclear pore complex by Hamed, Mohamed, Caspar, Birgit, Port, Sarah A, Kehlenbach, Ralph H

“…Nup214 is a major nucleoporin on the cytoplasmic side of the nuclear pore complex with roles in late steps of nuclear protein and mRNA export. It interacts…”
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Identification of CRM1-dependent Nuclear Export Cargos Using Quantitative Mass Spectrometry by Thakar, Ketan, Karaca, Samir, Port, Sarah A., Urlaub, Henning, Kehlenbach, Ralph H.

“…Chromosome region maintenance 1/exportin1/Exp1/Xpo1 (CRM1) is the major transport receptor for the export of proteins from the nucleus. It binds to nuclear…”
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Cargo Release from Myosin V Requires the Convergence of Parallel Pathways that Phosphorylate and Ubiquitylate the Cargo Adaptor by Wong, Sara, Hepowit, Nathaniel L., Port, Sarah A., Yau, Richard G., Peng, Yutian, Azad, Nadia, Habib, Alim, Harpaz, Nofar, Schuldiner, Maya, Hughson, Frederick M., MacGurn, Jason A., Weisman, Lois S.

“…Cellular function requires molecular motors to transport cargoes to their correct intracellular locations. The regulated assembly and disassembly of…”
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Analysis of CRM1-Dependent Nuclear Export in Permeabilized Cells by Kehlenbach, Ralph H, Port, Sarah A

“…Nuclear protein import and export assays in permeabilized cells have been instrumental for the identification of transport factors and for the molecular…”
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Human PDCD2L Is an Export Substrate of CRM1 That Associates with 40S Ribosomal Subunit Precursors by Landry-Voyer, Anne-Marie, Bilodeau, Sarah, Bergeron, Danny, Dionne, Kiersten L., Port, Sarah A., Rouleau, Caroline, Boisvert, François-Michel, Kehlenbach, Ralph H., Bachand, François

“…Protein arginine methyltransferase 3 (PRMT3) forms a stable complex with 40S ribosomal protein S2 (RPS2) and contributes to ribosome biogenesis. However, the…”
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Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary nuclear export complex by Monecke, Thomas, Dickmanns, Achim, Weiss, Manfred S., Port, Sarah A., Kehlenbach, Ralph H., Ficner, Ralf

“…High conformational flexibility is an intrinsic and indispensable property of nuclear transport receptors, which makes crystallization and structure…”
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Crystal structure of the 239 kDa nuclear export complex CRM1 - RanGTP - Snurportin1 - Nup214 - MBP by Ficner, Ralf, Monecke, Thomas, Port, Sarah A., Weiß, Manfred S., Kehlenbach, Ralph H., Dickmanns, Achim

“…Abstract only…”
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