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Journal of Biomedicine and Biotechnology
Volume 2011 (2011), Article ID 103069, 16 pages
Tropomodulin Capping of Actin Filaments in Striated Muscle Development and Physiology
Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
Received 30 June 2011; Accepted 18 August 2011
Academic Editor: Aikaterini Kontrogianni-Konstantopoulos
Copyright © 2011 David S. Gokhin and Velia M. Fowler. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Citations to this Article [20 citations]
The following is the list of published articles that have cited the current article.
- Sawako Yamashiro, David S. Gokhin, Sumiko Kimura, Roberta B. Nowak, and Velia M. Fowler, “Tropomodulins: Pointed-end capping proteins that regulate actin filament architecture in diverse cell types,” Cytoskeleton, vol. 69, no. 6, pp. 337–370, 2012.
- Xiao Zhao, Zheng Huang, Xiaohong Liu, Yaosheng Chen, Wen Gong, Kaifan Yu, Lijun Qin, Hu Chen, and Delin Mo, “The switch role of the Tmod4 in the regulation of balanced development between myogenesis and adipogenesis,” Gene, 2013.
- David S. Gokhin, and Velia M. Fowler, “A two-segment model for thin filament architecture in skeletal muscle,” Nature Reviews Molecular Cell Biology, vol. 14, no. 2, pp. 113–119, 2013.
- Thomas Fath, “Tropomodulins and tropomyosins - Organizers of cellular microcompartments,” Biomolecular Concepts, vol. 4, no. 1, pp. 89–101, 2013.
- Izabela Michalczyk, Aleksander F. Sikorski, Leszek Kotula, Richard P. Junghans, and Patrycja M. Dubielecka, “The emerging role of protein kinase Cθ in cytoskeletal signaling,” Journal of Leukocyte Biology, vol. 93, no. 3, pp. 319–327, 2013.
- Katherine T. Bliss, Takehiro Tsukada, Stefanie Mares Novak, Maxim V. Dorovkov, Samar P. Shah, Chinedu Nworu, Alla S. Kostyukova, and Carol C. Gregorio, “Phosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle,” Faseb Journal, vol. 28, no. 9, pp. 3987–3995, 2014.
- Raymond A. Lewis, Sawako Yamashiro, David S. Gokhin, and Velia M. Fowler, “Functional effects of mutations in the tropomyosin-binding sites of tropomodulin1 and tropomodulin3,” Cytoskeleton, vol. 71, no. 7, pp. 395–411, 2014.
- Sawako Yamashiro, David S. Gokhin, Zhenhua Sui, Sarah E. Bergeron, and Peter A. Rubenstein, “Differential Actin-regulatory Activities of Tropomodulin1 and Tropomodulin3 with Diverse Tropomyosin and Actin Isoforms*,” Journal of Biological Chemistry, vol. 289, no. 17, pp. 11616–11629, 2014.
- Caroline R. McKeown, Roberta B. Nowak, David S. Gokhin, and Velia M. Fowler, “Tropomyosin is required for cardiac morphogenesis, myofibril assembly, and formation of adherens junctions in the developing mouse embryo,” Developmental Dynamics, 2014.
- D. S. Gokhin, M. T. Tierney, Z. Sui, A. Sacco, and V. M. Fowler, “Calpain-mediated proteolysis of tropomodulin isoforms leads to thin filament elongation in dystrophic skeletal muscle,” Molecular Biology of the Cell, vol. 25, no. 6, pp. 852–865, 2014.
- Julien Ochala, David S. Gokhin, Hiroyuki Iwamoto, and Velia M. Fowler, “Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers,” Faseb Journal, vol. 28, no. 1, pp. 408–415, 2014.
- Weiyun Mu, Xifu Wang, Xiaolan Zhang, Sida Zhu, Dagong Sun, Weibo Ka, Lanping Amy Sung, and Weijuan Yao, “Fluid Shear Stress Upregulates E-Tmod41 via miR-23b-3p and Contributes to F-Actin Cytoskeleton Remodeling during Erythropoiesis,” Plos One, vol. 10, no. 8, 2015.
- David S. Gokhin, Julien Ochala, Andrea A. Domenighetti, and Velia M. Fowler, “Tropomodulin 1 directly controls thin filament length in both wild-type and tropomodulin 4-deficient skeletal muscle,” Development, vol. 142, no. 24, pp. 4351–4362, 2015.
- Teiji Oda, Akane Yamaguchi, Koji Shimizu, Tetsuro Nikai, and Ken-ichi Matsumoto, “Does the Rewarmed Heart Restore the Myocardial Proteome to That of the Pre-Cooled State? - A Proteomic Analysis of Surgical Samples,” Circulation Journal, vol. 79, no. 12, pp. 2648–+, 2015.
- Elisabeth Ehler, “Cardiac cytoarchitecture - why the “hardware” is important for heart function!,” Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2015.
- Christopher T. Pappas, Rachel M. Mayfield, Christine Henderson, Nima Jamilpour, Cathleen Cover, Zachary Hernandez, Kirk R. Hutchinson, Miensheng Chu, Ki-Hwan Nam, Jose M. Valdez, Pak Kin Wong, Henk L. Granzier, and Carol C. Gregorio, “Knockout of Lmod2 results in shorter thin filaments followed by dilated cardiomyopathy and juvenile lethality,” Proceedings of the National Academy of Sciences, vol. 112, no. 44, pp. 13573–13578, 2015.
- David S. Gokhin, and Velia M. Fowler, “Feisty filaments,” Current Opinion in Hematology, vol. 23, no. 3, pp. 206–214, 2016.
- Justin Kolb, Frank Li, Mei Methawasin, Maya Adler, Yael-Natalie Escobar, Joshua Nedrud, Christopher T. Pappas, Samantha P. Harris, and Henk Granzier, “Thin filament length in the cardiac sarcomere varies with sarcomere length but is independent of titin and nebulin,” Journal of Molecular and Cellular Cardiology, 2016.
- Lise Mazelet, Matthew O. Parker, Mei Li, Anders Arner, and Rachel Ashworth, “Role of Active Contraction and Tropomodulins in Regulating Actin Filament Length and Sarcomere Structure in Developing Zebrafish Skeletal Muscle,” Frontiers in Physiology, vol. 7, 2016.
- A. Maerkens, M. Olivé, A. Schreiner, S. Feldkirchner, J. Schessl, J. Uszkoreit, K. Barkovits, A. K. Güttsches, V. Theis, M. Eisenacher, M. Tegenthoff, L. G. Goldfarb, R. Schröder, B. Schoser, P. F. M. van der Ven, D. O. Fürst, M. Vorgerd, K. Marcus, and R. A. Kley, “New insights into the protein aggregation pathology in myotilinopathy by combined proteomic and immunolocalization analyses,” Acta Neuropathologica Communications, vol. 4, no. 1, 2016.