The Kinase Domain of Titin Controls Muscle Gene Expression and Protein Turnover

By S. Lange, F. Xiang, A. Yakovenko, A. Vihola, P. Hackman, E. Rostkova, Jakob Kristensen, B. Brandmeier, Gereon Franzen, B. Hedberg and 9 more. Science, 2005

608 citations recorded by the source corpus.

Subfields: Cardiology and Cardiovascular Medicine, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e433047b5703f73a539ac7543a3cb4191ef02104

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In Cardiology and Cardiovascular Medicine

In Molecular Biology

Citations in the corpus

The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. (2007, background): “…muscle atrophy does not eliminate the possibility that MuRF1 acts on additional important substrates—and the prior report that a MuRF family member can perturb serum response factor (SRF) (Lange et al., 2005) makes one wonder whether MuRF1 also functions away from the sarcomere during atrophy.”
Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus (2009, background): “This force transfer might function analogously to the way in which stress-induced distortion of cytoskeletal titin influences the nuclear translocation of MURF2 (also known as TRIM55 ), which is a ligand of the transactivation domain of the serum response transcription factor SR”
Truncations of Titin Causing Dilated Cardiomyopathy (2012, unknown): “(%) 11 (30) 17 (31) 2 (12) 14 (26) 4 (31) 56 (41)”
Sense and stretchability: the role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction. (2007, background): “Activation of the kinase by stretch allows interaction with the proteins Nbr1 and p62, the latter binding to MURF-2 (Figure 2).(28) MURF-2 then interacts with SRF to inhibit its nuclear localization and transcriptional activity, hence suppressing hypertrophic responses elicited by mechanical forces.”
A role for ubiquitin in selective autophagy. (2009, background): “Given the remarkable similarity in the domain organization (Figure 1) and direct interaction with p62, NBR1 has subsequently been studied in cell signaling and differentiation: in muscle cells, NBR1 is a signaling mediator downstream of the giant kinase titin (Lange et al., 2005).”
Transcriptional mechanisms regulating skeletal muscle differentiation, growth and homeostasis (2011, background): “At the M-band, the mechanically modulated kinase domain of titin interacts with a complex of the protein products of the atrogenes NBR1, SQSTM1 and the MURF”
Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. (2014, background): “…MURF2, and KEAP1, are among the direct interaction partners of p62 (Fusco et al., 2012; Jain et al., 2010; Komatsu et al., 2010; Lange et al., 2005; Lau et al., 2010; Moscat and Diaz-Meco, 2009), which may promote ubiquitination of p62 substrates, impacting inclusion body formation and aggrephagy.”