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Open AccessArticle

Exploring Obscurin and SPEG Kinase Biology

1
Department of Biology, University of Konstanz, 78457 Konstanz, Germany
2
Centre for Molecular and Translational Medicine, The Wallenberg Laboratory and Wallenberg, Department of Molecular and Clinical Medicine, University of Gothenburg, 41345 Gothenburg, Sweden
3
Department of Medicine, University of California, San Diego, CA 92093, USA
4
Department of Clinical Physiology, Sahlgrenska University Hospital, 41345 Gothenburg, Sweden
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editors: Tommaso Angelone and Julius Bogomolovas
J. Clin. Med. 2021, 10(5), 984; https://doi.org/10.3390/jcm10050984
Received: 30 December 2020 / Revised: 10 February 2021 / Accepted: 18 February 2021 / Published: 2 March 2021
(This article belongs to the Special Issue Protein Kinases in Cardiovascular Pathophysiology)
Three members of the obscurin protein family that contain tandem kinase domains with important signaling functions for cardiac and striated muscles are the giant protein obscurin, its obscurin-associated kinase splice isoform, and the striated muscle enriched protein kinase (SPEG). While there is increasing evidence for the specific roles that each individual kinase domain plays in cross-striated muscles, their biology and regulation remains enigmatic. Our present study focuses on kinase domain 1 and the adjacent low sequence complexity inter-kinase domain linker in obscurin and SPEG. Using Phos-tag gels, we show that the linker in obscurin contains several phosphorylation sites, while the same region in SPEG remained unphosphorylated. Our homology modeling, mutational analysis and molecular docking demonstrate that kinase 1 in obscurin harbors all key amino acids important for its catalytic function and that actions of this domain result in autophosphorylation of the protein. Our bioinformatics analyses also assign a list of putative substrates for kinase domain 1 in obscurin and SPEG, based on the known and our newly proposed phosphorylation sites in muscle proteins, including obscurin itself. View Full-Text
Keywords: obscurin; striated muscle enriched protein kinase; SPEG; kinase obscurin; striated muscle enriched protein kinase; SPEG; kinase
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MDPI and ACS Style

Fleming, J.R.; Rani, A.; Kraft, J.; Zenker, S.; Börgeson, E.; Lange, S. Exploring Obscurin and SPEG Kinase Biology. J. Clin. Med. 2021, 10, 984. https://doi.org/10.3390/jcm10050984

AMA Style

Fleming JR, Rani A, Kraft J, Zenker S, Börgeson E, Lange S. Exploring Obscurin and SPEG Kinase Biology. Journal of Clinical Medicine. 2021; 10(5):984. https://doi.org/10.3390/jcm10050984

Chicago/Turabian Style

Fleming, Jennifer R.; Rani, Alankrita; Kraft, Jamie; Zenker, Sanja; Börgeson, Emma; Lange, Stephan. 2021. "Exploring Obscurin and SPEG Kinase Biology" J. Clin. Med. 10, no. 5: 984. https://doi.org/10.3390/jcm10050984

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