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11 results on '"Beck, Gisela"'

1. Nucleobindin-1 regulates ECM degradation by promoting intra-Golgi trafficking of MMPs

Author

Pacheco-Fernandez, Natalia, primary, Pakdel, Mehrshad, primary, Blank, Birgit, primary, Sanchez-Gonzalez, Ismael, primary, Weber, Kathrin, primary, Tran, Mai Ly, primary, Hecht, Tobias Karl-Heinz, primary, Gautsch, Renate, primary, Beck, Gisela, primary, Perez, Franck, primary, Hausser, Angelika, primary, Linder, Stefan, primary, and von Blume, Julia, primary

Published
2020
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2. Fam20C regulates protein secretion by Cab45 phosphorylation

Author

Hecht, Tobias Karl-Heinz, primary, Blank, Birgit, additional, Steger, Martin, additional, Lopez, Victor, additional, Beck, Gisela, additional, Ramazanov, Bulat, additional, Mann, Matthias, additional, Tagliabracci, Vincent, additional, and von Blume, Julia, additional

Published
2020
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3. Secretory cargo sorting by Ca2+-dependent Cab45 oligomerization at the trans-Golgi network

Author

Crevenna, Alvaro H., primary, Blank, Birgit, additional, Maiser, Andreas, additional, Emin, Derya, additional, Prescher, Jens, additional, Beck, Gisela, additional, Kienzle, Christine, additional, Bartnik, Kira, additional, Habermann, Bianca, additional, Pakdel, Mehrshad, additional, Leonhardt, Heinrich, additional, Lamb, Don C., additional, and von Blume, Julia, additional

Published
2016
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4. Isotropic actomyosin dynamics promote organization of the apical cell cortex in epithelial cells

Author

Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Laboratory for Computational Cell Biology & Biophysics, Bathe, Mark, Diesinger, Philipp M., Klingner, Christoph, Cherian, Anoop V., Fels, Johannes, Aufschnaiter, Roland, Maghelli, Nicola, Keil, Thomas, Beck, Gisela, Tolic-Norrelykke, Iva M., Wedlich-Soldner, Roland, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Laboratory for Computational Cell Biology & Biophysics, Bathe, Mark, Diesinger, Philipp M., Klingner, Christoph, Cherian, Anoop V., Fels, Johannes, Aufschnaiter, Roland, Maghelli, Nicola, Keil, Thomas, Beck, Gisela, Tolic-Norrelykke, Iva M., and Wedlich-Soldner, Roland

Abstract

Although cortical actin plays an important role in cellular mechanics and morphogenesis, there is surprisingly little information on cortex organization at the apical surface of cells. In this paper, we characterize organization and dynamics of microvilli (MV) and a previously unappreciated actomyosin network at the apical surface of Madin–Darby canine kidney cells. In contrast to short and static MV in confluent cells, the apical surfaces of nonconfluent epithelial cells (ECs) form highly dynamic protrusions, which are often oriented along the plane of the membrane. These dynamic MV exhibit complex and spatially correlated reorganization, which is dependent on myosin II activity. Surprisingly, myosin II is organized into an extensive network of filaments spanning the entire apical membrane in nonconfluent ECs. Dynamic MV, myosin filaments, and their associated actin filaments form an interconnected, prestressed network. Interestingly, this network regulates lateral mobility of apical membrane probes such as integrins or epidermal growth factor receptors, suggesting that coordinated actomyosin dynamics contributes to apical cell membrane organization., Max Planck Society for the Advancement of Science, German Research Foundation (SFB863), University of Münster. Cells-in-Motion Cluster of Excellence (EXC1003-CiM)

Published
2014

9. Lifeact mice for studying F-actin dynamics

Author

Riedl, Julia, primary, Flynn, Kevin C, additional, Raducanu, Aurelia, additional, Gärtner, Florian, additional, Beck, Gisela, additional, Bösl, Michael, additional, Bradke, Frank, additional, Massberg, Steffen, additional, Aszodi, Attila, additional, Sixt, Michael, additional, and Wedlich-Söldner, Roland, additional

Published
2010
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10. Secretory cargo sorting by Ca2+-dependent Cab45 oligomerization at the trans-Golgi network.

Author

Crevenna, Alvaro H., Blank, Birgit, Maiser, Andreas, Emin, Derya, Prescher, Jens, Beck, Gisela, Kienzle, Christine, Bartnik, Kira, Habermann, Bianca, Pakdel, Mehrshad, Leonhardt, Heinrich, Lamb, Don C., and von Blume, Julia

Subjects
*OLIGOMERIZATION, *CALCIUM channels, *ION channels, *MEMBRANE proteins, *BIOLOGICAL membranes
Abstract

Sorting and export of transmembrane cargoes and lysosomal hydrolases at the trans-Golgi network (TGN) are well understood. However, elucidation of the mechanism by which secretory cargoes are segregated for their release into the extracellular space remains a challenge. We have previously demonstrated that, in a reaction that requires Ca2+, the soluble TGN-resident protein Cab45 is necessary for the sorting of secretory cargoes at the TGN. Here, we report that Cab45 reversibly assembles into oligomers in the presence of Ca2+. These Cab45 oligomers specifically bind secretory proteins, such as COMP and LyzC, in a Ca2+-dependent manner in vitro. In intact cells, mutation of the Ca2+-binding sites in Cab45 impairs oligomerization, as well as COMP and LyzC sorting. Superresolution microscopy revealed that Cab45 colocalizes with secretory proteins and the TGN Ca2+ pump (SPCA1) in specific TGN microdomains. These findings reveal that Ca2+-dependent changes in Cab45 mediate sorting of specific cargo molecules at the TGN. [ABSTRACT FROM AUTHOR]

Published
2016
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11. Cofilin recruits F-actin to SPCA1 and promotes Ca2+-mediated secretory cargo sorting.

Author

Kienzle, Christine, Basnet, Nirakar, Crevenna, Alvaro H., Beck, Gisela, Habermann, Bianca, Naoko Mizu, and von Blume, Julia

Subjects
*ACTIN research, *PROTEIN research, *ADENOSINE triphosphatase, *GOLGINS, *AMINO acids, *PHOSPHORYLATION
Abstract

The actin filament severing protein cofilin-1 (CFL-1) is required for actin and P-type ATPase secretory pathway calcium ATPase (SPCA)-dependent sorting of secretory proteins at the trans-Golgi network (TGN). How these proteins interact and activate the pump to facilitate cargo sorting, however, is not known. We used purified proteins to assess interaction of the cytoplasmic domains of SPCA1 with actin and CFL-1. A 132-amino acid portion of the SPCA1 phosphorylation domain (P-domain) interacted with actin in a CFL-1-dependent manner. This domain, coupled to nickel nitrilotriacetic acid (Ni-NTA) agarose beads, specifically recruited F-actin in the presence of CFL-1 and, when expressed in HeLa cells, inhibited Ca2+ entry into the TGN and secretory cargo sorting. Mutagenesis of four amino acids in SPCA1 that represent the CFL-1 binding site also affected Ca2+ import into the TGN and secretory cargo sorting. Altogether, our findings reveal the mechanism of CFL-1-dependent recruitment of actin to SPCA1 and the significance of this interaction for Ca2+ influx and secretory cargo sorting. [ABSTRACT FROM AUTHOR]

Published
2014
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