Histidine-rich Ca-binding protein interacts with sarcoplasmic reticulum Ca-ATPase

Arvanitis, Demetrios A.; Vafiadaki, Elizabeth; Fan, Guo-Chang; Mitton, Bryan; Gregory, Kimberly N.; Monte, Federica del; Kontrogianni‐Konstantopoulos, Aikaterini; Sanoudou, Despina; Kranias, Evangelia G.

doi:10.1152/ajpheart.00278.2007

Cited by 80 publications

(110 citation statements)

References 41 publications

(64 reference statements)

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“…It has been also reported that calreticulin is associated with SERCA2a, in response to oxidative stress (50). Other luminal proteins like sarcalumenin and HRC interact with SERCA2 and regulate its activity (17,18). HRC interacts with the luminal loop L1 of SERCA2 and inhibits SERCA2 activity in cardiomyocytes, whereas the interaction site of SERCA2 with sarcalumenin is not known yet (17).…”

Section: Discussionmentioning

confidence: 99%

“…Recent studies have suggested that SR luminal proteins such as calreticulin (15), ER protein 57 (16), sarcalumenin (17), histidine-rich Ca 2ϩ -binding protein (HRC) (18), and calumenin (1) interact with SERCA2. HRC binds to SERCA2 in a Ca 2ϩ -dependent manner, and its overexpression could inhibit SERCA2 activity and Ca 2ϩ cycling in cardiomyocytes (18,19). Sarcalumenin also interacts with SERCA2, which may consequently increase the tendency of its retention in the SR lumen and increase the SERCA2 protein stability (17).…”

Section: Calumenin Is a Multiple Ef-handmentioning

confidence: 99%

“…EF-hand protein S100A1 interacts with SERCA2 in the cytosolic side and regulates contractility in heart (14). Recent studies have suggested that SR luminal proteins such as calreticulin (15), ER protein 57 (16), sarcalumenin (17), histidine-rich Ca 2ϩ -binding protein (HRC) (18), and calumenin (1) interact with SERCA2. HRC binds to SERCA2 in a Ca 2ϩ -dependent manner, and its overexpression could inhibit SERCA2 activity and Ca 2ϩ cycling in cardiomyocytes (18,19).…”

Section: From the Department Of Life Science And Systems Biology Resementioning

confidence: 99%

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Characterization of Calumenin-SERCA2 Interaction in Mouse Cardiac Sarcoplasmic Reticulum

Sahoo

Kim

Kang

et al. 2009

Journal of Biological Chemistry

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Calumenin is a multiple EF-handSarco(endo)plasmic reticulum Ca 2ϩ -ATPase (SERCA) 2 is a major player in muscle relaxation of mammalian heart (2). Tight regulation of SERCA activity is important for normal Ca 2ϩ homeostasis in heart, and altered activity could lead to impaired excitation-contraction (E-C) coupling and cardiac diseases (3). SERCA2a is the predominant isoform in mouse heart, compared with SERCA2b (4). SERCA2a and SERCA2b are identical up to 994 amino acids. However, the C terminus of SERCA2b contains additional 50 amino acids, as compared with only 4 amino acids in SERCA2a (5). Structural and biochemical studies have shown that SERCA2 contains 10 transmembrane segments (M1-10), and the large globular cytoplasmic part is composed of three domains: the ␤ strand domain between M2 and M3, the phosphorylation domain attached to M4 at one end, and the nucleotide binding domain at the other end. The nucleotide binding domain contains a hinge domain, which is connected to the M5 segment (6). The luminal side contains five luminal domains connecting the following segments M1 and M2, M3 and M4, M5 and M6, M7 and M8, and M9 and M10, respectively (6 -8).Recent studies have shown that a number of proteins interact with SERCA2 and regulate its stability and activity. Among them phospholamban (PLN) is the most extensively studied molecule (9). PLN interacts with SERCA2 and decreases apparent affinity of SERCA2 for Ca 2ϩ , and this inhibition can be disrupted by phosphorylation of PLN or by elevation of cytosolic Ca 2ϩ , which leads to reversal of the inhibition (10). PLN is the important regulator of SERCA activity and contractility in heart (11). Other proteins related to the apoptotic pathway such as Bcl2 (12) and Hax1(13) interact with SERCA2 in the cytosolic side of SERCA2 and regulate SERCA2 protein level and stability. EF-hand protein S100A1 interacts with SERCA2 in the cytosolic side and regulates contractility in heart (14). Recent studies have suggested that SR luminal proteins such as calreticulin (15), ER protein 57 (16), sarcalumenin (17), histidine-rich Ca 2ϩ -binding protein (HRC) (18), and calumenin (1) interact with SERCA2. HRC binds to SERCA2 in a Ca 2ϩ -dependent manner, and its overexpression could inhibit SERCA2 activity and Ca 2ϩ cycling in cardiomyocytes (18,19). Sarcalumenin also interacts with SERCA2, which may consequently increase the tendency of its retention in the SR lumen and increase the SERCA2 protein stability (17).Calumenin is a multiple EF-hand Ca 2ϩ -binding protein and is found to have unique C-terminal SR retention signal HDEF (20,21). Calumenin is associated with the ryanodine receptor (RyR) in rabbit skeletal muscle, and its overexpression shows decreased depolarization-induced Ca 2ϩ release in C2C12 myotubes (22

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Section: Discussionmentioning

confidence: 99%

Section: Calumenin Is a Multiple Ef-handmentioning

confidence: 99%

Section: From the Department Of Life Science And Systems Biology Resementioning

confidence: 99%

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Characterization of Calumenin-SERCA2 Interaction in Mouse Cardiac Sarcoplasmic Reticulum

Sahoo

Kim

Kang

et al. 2009

Journal of Biological Chemistry

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“…Early evidence showed that HRC, via its glutamate-enriched carboxy-terminal region, interacts with triadin in a Ca 2þ -dependent manner to anchor HRC to the junctional membrane (Sacchetto et al 1999;Lee et al 2001;Sacchetto et al 2001); this led to the hypothesis that HRC may also be responsible for regulating RyR activity through its interactions with triadin. HRC also interacts with SERCA in cardiac muscle (Arvanitis et al 2007), leading to the intriguing hypothesis that HRC may link Ca 2þ release (via triadin) and Ca 2þ uptake (via SERCA) in the SR lumen (Pritchard and Kranias 2009). HRC is implicated in cardiovascular disease: overexpression (gain-of-function) of HRC provides protection against heart damage induced by ischemia/reperfusion (Zhou et al 2007) whereas a S 96 A mutation in HRC has been identified in human patients to correlate with decreased survival in idiopathic dilated cardiomyopathy (Arvanitis et al 2008).…”

Section: Minor Sr Ca 2þ Buffering Proteinsmentioning

confidence: 99%

Organellar Calcium Buffers

Prins¹,

Michalak²

2011

Cold Spring Harbor Perspectives in Biology

120

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“…The blot overlay assays were performed as previously described (10). Briefly, aliquots containing ϳ2.5 g of affinity-purified GST, GST-CFL2-A (aa 1 to 55), GST-CFL2-B (aa 55 to 108), and GST-CFL2-C (aa 105 to 166) fusion proteins were separated by 10% SDS-PAGE and transferred to nitrocellulose membranes.…”

mentioning

confidence: 99%

Muscle Lim Protein Interacts with Cofilin 2 and Regulates F-Actin Dynamics in Cardiac and Skeletal Muscle

Papalouka

Arvanitis

Vafiadaki

et al. 2009

Molecular and Cellular Biology

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The muscle LIM protein (MLP) and cofilin 2 (CFL2) are important regulators of striated myocyte function. Mutations in the corresponding genes have been directly associated with severe human cardiac and skeletal myopathies, and aberrant expression patterns have often been observed in affected muscles. Herein, we have investigated whether MLP and CFL2 are involved in common molecular mechanisms, which would promote our understanding of disease pathogenesis. We have shown for the first time, using a range of biochemical and immunohistochemical methods, that MLP binds directly to CFL2 in human cardiac and skeletal muscles. The interaction involves the inter-LIM domain, amino acids 94 to 105, of MLP and the amino-terminal domain, amino acids 1 to 105, of CFL2, which includes part of the actin depolymerization domain. The MLP/CFL2 complex is stronger in moderately acidic (pH 6.8) environments and upon CFL2 phosphorylation, while it is independent of Ca 2؉ levels. This interaction has direct implications in actin cytoskeleton dynamics in regulating CFL2-dependent F-actin depolymerization, with maximal depolymerization enhancement at an MLP/ CFL2 molecular ratio of 2:1. Deregulation of this interaction by intracellular pH variations, CFL2 phosphorylation, MLP or CFL2 gene mutations, or expression changes, as observed in a range of cardiac and skeletal myopathies, could impair F-actin depolymerization, leading to sarcomere dysfunction and disease.The muscle LIM protein (MLP) has emerged as a critical player in striated muscle physiology and pathophysiology over recent years. MLP, encoded by the CSRP3 (or CRP3) gene, is a member of the conserved LIM-only protein family since it contains two LIM functional zinc finger domains, and it is expressed exclusively in muscle cells. Specifically, in differentiating striated muscle cells, MLP localizes in the nucleus, promoting myogenic differentiation (8), while in adult muscle, it translocates to the cytoplasm and assumes an essential role in myocyte cytoarchitecture. Through its interactions with structural proteins, such as alpha-actinin, telethonin (T-cap), ␤I-spectrin, and N-RAP, MLP has been suggested to act as a scaffold protein for the basic contractile unit, the sarcomere, and the actin-based cytoskeleton (7,9,25,27,46,73).Mutations in CSRP3 have been directly associated with dilated (DCM) and hypertrophic (HCM) cardiomyopathies (9,31,32,46). HCM is the most common genetic myocardial disease, with a prevalence of 0.2% in adults, and the most frequent cause of sudden cardiac death in young individuals, while DCM is the third most common cause of heart failure (54,55,76). Genetic aberrations in MLP have been shown to lead to marked actin cytoskeleton disorganization and disrupted cardiac myofibrillar cytoarchitecture (9). Similar observations have been described for skeletal muscles, and HCM-CSRP3 mutations have been associated with mild skeletal myopathy (9, 31). Various hypotheses, including an MLP role in mechanical stretch sensing or the mechanical stress response, have...

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Histidine-rich Ca-binding protein interacts with sarcoplasmic reticulum Ca-ATPase

Cited by 80 publications

References 41 publications

Characterization of Calumenin-SERCA2 Interaction in Mouse Cardiac Sarcoplasmic Reticulum

Characterization of Calumenin-SERCA2 Interaction in Mouse Cardiac Sarcoplasmic Reticulum

Organellar Calcium Buffers

Muscle Lim Protein Interacts with Cofilin 2 and Regulates F-Actin Dynamics in Cardiac and Skeletal Muscle

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