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The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics

Max Planck Institute of Psychiatry, Kraepelinstraße 2-10, 80805 München, Germany
Department of Psychiatry and Psychotherapy & Focus Program Translational Neuroscience, Johannes Gutenberg Universität Medical Center, 55131 Mainz, Germany
Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, University of Barcelona, IDIBAPS, CIBERNED, Casanova, 143, 08036 Barcelona, Spain
Lehrstuhl für Biophysik E27, Technische Universität München, 85748 Garching, Germany
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(12), 3993;
Received: 29 October 2018 / Revised: 7 December 2018 / Accepted: 10 December 2018 / Published: 11 December 2018
(This article belongs to the Special Issue Molecular Psychiatry)
Cytoskeletal dynamics are pivotal to memory, learning, and stress physiology, and thus psychiatric diseases. Downregulated in renal cell carcinoma 1 (DRR1) protein was characterized as the link between stress, actin dynamics, neuronal function, and cognition. To elucidate the underlying molecular mechanisms, we undertook a domain analysis of DRR1 and probed the effects on actin binding, polymerization, and bundling, as well as on actin-dependent cellular processes. Methods: DRR1 domains were cloned and expressed as recombinant proteins to perform in vitro analysis of actin dynamics (binding, bundling, polymerization, and nucleation). Cellular actin-dependent processes were analyzed in transfected HeLa cells with fluorescence recovery after photobleaching (FRAP) and confocal microscopy. Results: DRR1 features an actin binding site at each terminus, separated by a coiled coil domain. DRR1 enhances actin bundling, the cellular F-actin content, and serum response factor (SRF)-dependent transcription, while it diminishes actin filament elongation, cell spreading, and actin treadmilling. We also provide evidence for a nucleation effect of DRR1. Blocking of pointed end elongation by addition of profilin indicates DRR1 as a novel barbed end capping factor. Conclusions: DRR1 impacts actin dynamics in several ways with implications for cytoskeletal dynamics in stress physiology and pathophysiology. View Full-Text
Keywords: stress physiology; cytoskeleton; actin dynamics; DRR1; TU3A; FAM107A stress physiology; cytoskeleton; actin dynamics; DRR1; TU3A; FAM107A
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MDPI and ACS Style

Kretzschmar, A.; Schülke, J.-P.; Masana, M.; Dürre, K.; Müller, M.B.; Bausch, A.R.; Rein, T. The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics. Int. J. Mol. Sci. 2018, 19, 3993.

AMA Style

Kretzschmar A, Schülke J-P, Masana M, Dürre K, Müller MB, Bausch AR, Rein T. The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics. International Journal of Molecular Sciences. 2018; 19(12):3993.

Chicago/Turabian Style

Kretzschmar, Anja, Jan-Philip Schülke, Mercè Masana, Katharina Dürre, Marianne B. Müller, Andreas R. Bausch, and Theo Rein. 2018. "The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics" International Journal of Molecular Sciences 19, no. 12: 3993.

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