CacyBP/SIP as a novel modulator of the thin filament.
Ewelina Jurewicz,Zofia Ostrowska,Jolanta Jozwiak,Maria Jolanta Redowicz,Wieslawa Lesniak,Joanna Moraczewska,Anna Filipek +6 more
TLDR
The results suggest that CacyBP/SIP, through its interaction with both actin and tropomyosin, regulates the organization and functional properties of the thin filament.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2013-03-01 and is currently open access. It has received 18 citations till now. The article focuses on the topics: Tropomyosin & Actin.read more
Citations
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Non-nuclear function of sumoylated proteins.
Urszula Wasik,Anna Filipek +1 more
TL;DR: This review summarized the results describing the non-nuclear role of SUMO substrates in the regulation of channel activity, receptor function, G-protein signaling, activity of enzymes, cytoskeletal organization, exocytosis, autophagy and mitochondrial dynamics.
Journal ArticleDOI
CacyBP/SIP--Structure and variety of functions.
TL;DR: Detailed characterization of the physical, biochemical and biological properties of CacyBP/SIP will provide better insight into the regulation of its diverse functions in vivo, and will help clarify the potential of therapeutic targeting of this protein.
Journal ArticleDOI
Expression of genes encoding the calcium signalosome in cellular and transgenic models of Huntington's disease.
Magdalena Czeredys,Joanna Gruszczynska-Biegala,Teresa Schacht,Axel Methner,Jacek Kuznicki,Jacek Kuznicki +5 more
TL;DR: The data indicate that the dysregulation of calcium homeostasis correlates with changes in the gene expression of members of the calciosome, however, differed in the two models of HD used in this study, indicating that each HD model exhibits distinct features that may only partially resemble the human disease.
Journal ArticleDOI
Dysregulation of Neuronal Calcium Signaling via Store-Operated Channels in Huntington's Disease.
TL;DR: In this paper, a review of recent studies that revealed a relationship between HD pathology and elevations of store-operated Ca2+ entry (SOCE) in different models of HD, including YAC128 mice (a transgenic model of HD), cellular HD models, and induced pluripotent stem cell (iPSC)-based GABAergic medium spiny neurons (MSNs) that are obtained from adult HD patient fibroblasts.
Journal ArticleDOI
Dimerization and phosphatase activity of calcyclin-binding protein/Siah-1 interacting protein: the influence of oxidative stress
Agnieszka M. Topolska-Woś,Steven M. Shell,Ewa Kilanczyk,Roman H. Szczepanowski,Walter J. Chazin,Anna Filipek +5 more
TL;DR: The results suggest that dimerization is important for controlling phosphatase activity of CacyBP/SIP and for regulating the ERK1/2 signaling pathway.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Book
Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Book ChapterDOI
Use of T7 RNA polymerase to direct expression of cloned genes.
Journal ArticleDOI
The Regulation of Rabbit Skeletal Muscle Contraction I. BIOCHEMICAL STUDIES OF THE INTERACTION OF THE TROPOMYOSIN-TROPONIN COMPLEX WITH ACTIN AND THE PROTEOLYTIC FRAGMENTS OF MYOSIN
James A. Spudich,Susan Watt +1 more
TL;DR: Actin purified by a new, simple, and rapid purification procedure activated the ATPase activity of both heavy meromyosin and Subfragment 1 of heavy mercyosin, and this activation was not inhibited by the removal of Ca2+.
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Molecular cloning and expression of a mouse brain cDNA encoding a novel protein target of calcyclin.
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