The potential mechanism of action of Sorcin and its interacting proteins

Murata, Jun; Fei, Ling; Sanches, Jaceline Gislaine Pires; Yu, Xiao; Wei, Yiran; Zhang, Jun

doi:10.1016/j.cca.2020.09.011

Cited by 9 publications

(7 citation statements)

References 43 publications

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“…PABP1 is one of the "TOP" (terminal oligopyrimidine) class mRNA-encoded proteins, which includes components of translational machinery and may play important roles in synaptic plasticity and cognitive function (Tsokas, Ma, Iyengar, Landau, & Blitzer, 2007;Wells et al, 2001). which is a calcium-binding protein highly expressed in both brain and heart (Ilari et al, 2015;Mao et al, 2020). Previous studies indicate that Sorcin increases Ca 2+ accumulation in the endoplasmic (ER) and mitochondria.…”

Section: Resultsmentioning

confidence: 99%

“…Downregulation of four proteins is overlapped in AMPKα1 cKO and α2 cKO mice: 116 kDa U5 small nuclear ribonucleoprotein component (O08810), Cullin‐3 (Q9JLV5), Sorcin (Q6P069), and monoglyceride lipase (Q35678). One protein of interest from the neuroscience perspective is Sorcin (soluble resistance‐related calcium binding protein), which is a calcium‐binding protein highly expressed in both brain and heart (Ilari et al, 2015; Mao et al, 2020). Previous studies indicate that Sorcin increases Ca 2+ accumulation in the endoplasmic (ER) and mitochondria.…”

Section: Resultsmentioning

confidence: 99%

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Protein expression alteration in hippocampus upon genetic repression of AMPKα isoforms

et al. 2021

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The AMP-activated protein kinase (AMPK) is a molecular sensor to help maintain cellular energy homeostasis. AMPK is a heterotrimeric complex and its enzymatic catalytic subunit includes two isoforms: α1 and α2. Dysregulation of AMPK signaling is linked to neuronal diseases characterized with cognitive impairments. Emerging evidence also suggest isoform-specific roles of AMPK in the brain. AMPK regulates protein synthesis, which is critical for memory formation and neuronal plasticity. However, the consequence of altering AMPK activity on the translation of specific proteins in the brain is unknown. Here, we use unbiased mass spectrometry-based proteomics approach to analyze protein profile alterations in hippocampus and prefrontal cortex of transgenic mice in which the genes for the two AMPKα isoforms are conditionally deleted. The study revealed identities of proteins whose expression is sensitive to suppression of AMPKα1 and/or α2 isoform. These data may serve as a basis for future in-depth study. Elucidation of the functional relevance of the alteration of specific proteins could provide insights into identification of novel therapeutic targets for neuronal disorders characterized with AMPK signaling dysregulation and impaired cellular energy metabolism.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Protein expression alteration in hippocampus upon genetic repression of AMPKα isoforms

et al. 2021

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“…Some proteins exert their regulatory effects by activating or inhibiting proteins they interact with. In recent years, the role of PPI in the development of tumors is increasingly well-appreciated [ 60 ]. The first 31 amino-acid fragments in the amino-terminal of ANXA7 can be combined with SRI, and the carboxyl-terminal of ANXA7 can be combined with calcium ions to form a protein complex to exert the biological effects [ 37 , 59 ].…”

Section: Discussionmentioning

confidence: 99%

AnnexinA7 promotes epithelial–mesenchymal transition by interacting with Sorcin and contributes to aggressiveness in hepatocellular carcinoma

et al. 2021

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Hepatocellular carcinoma (HCC) is one of the most common cancers worldwide, and metastasis is the major cause of the high mortality of HCC. In this study, we identified that AnnexinA7 (ANXA7) and Sorcin (SRI) are overexpressed and interacting proteins in HCC tissues and cells. In vitro functional investigations revealed that the interaction between ANXA7 and SRI regulated epithelial–mesenchymal transition (EMT), and then affected migration, invasion, and proliferation in HCC cells. Furthermore overexpression/knockdown of ANXA7 was remarkably effective in promoting/inhibiting tumorigenicity and EMT in vivo. Altogether, our study unveiled a mechanism that ANXA7 promotes EMT by interacting with SRI and further contributes to the aggressiveness in HCC, which provides a novel potential therapeutic target for preventing recurrence and metastasis in HCC.

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“…There are two main isoforms, the 22 kDa isoform which is the most abundant one and is found in the cytosol, and the 18 kDa isoform, which is localized in the mitochondria [ 1 ]. Mass spectrometry analysis and database searching have revealed that sorcin is widely expressed in most human tissues, such as skeletal muscle, kidney, brain, cardiac muscle, breast and skin [ 2 , 3 ], and it is overexpressed in a variety of human tumors and human cancer cell lines [ 4 , 5 , 6 ]. Binding of calcium ions (Ca 2+ ) is essential to translocate sorcin from the cytoplasm to the cell membrane, and there it can interact with other membrane proteins involved in Ca 2+ homeostasis [ 2 , 7 ].…”

Section: Introductionmentioning

confidence: 99%

“…Binding of calcium ions (Ca 2+ ) is essential to translocate sorcin from the cytoplasm to the cell membrane, and there it can interact with other membrane proteins involved in Ca 2+ homeostasis [ 2 , 7 ]. Through the binding of Ca 2+ to sorcin, this protein plays a significant role in cancer cells [ 8 ], and in the regulation of angiogenesis [ 9 ], mitosis [ 10 ] and endoplasmic reticulum (ER) stress [ 11 ], as revised in Colotti et al [ 2 ] and Mao et al [ 3 ]. The involvement of sorcin in apoptosis [ 12 ] and in metastasis of several cancer types has also been described [ 13 , 14 ].…”

Section: Introductionmentioning

confidence: 99%

Sorcin Activates the Brain PMCA and Blocks the Inhibitory Effects of Molecular Markers of Alzheimer’s Disease on the Pump Activity

Berrocal

Saez

Mata

2021

IJMS

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Since dysregulation of intracellular calcium (Ca2+) levels is a common occurrence in neurodegenerative diseases, including Alzheimer’s disease (AD), the study of proteins that can correct neuronal Ca2+ dysregulation is of great interest. In previous work, we have shown that plasma membrane Ca2+-ATPase (PMCA), a high-affinity Ca2+ pump, is functionally impaired in AD and is inhibited by amyloid-β peptide (Aβ) and tau, two key components of pathological AD hallmarks. On the other hand, sorcin is a Ca2+-binding protein highly expressed in the brain, although its mechanism of action is far from being clear. Sorcin has been shown to interact with the intracellular sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA), and other modulators of intracellular Ca2+ signaling, such as the ryanodine receptor or presenilin 2, which is closely associated with AD. The present work focuses on sorcin in search of new regulators of PMCA and antagonists of Aβ and tau toxicity. Results show sorcin as an activator of PMCA, which also prevents the inhibitory effects of Aβ and tau on the pump, and counteracts the neurotoxicity of Aβ and tau by interacting with them.

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The potential mechanism of action of Sorcin and its interacting proteins

Cited by 9 publications

References 43 publications

Protein expression alteration in hippocampus upon genetic repression of AMPKα isoforms

Protein expression alteration in hippocampus upon genetic repression of AMPKα isoforms

AnnexinA7 promotes epithelial–mesenchymal transition by interacting with Sorcin and contributes to aggressiveness in hepatocellular carcinoma

Sorcin Activates the Brain PMCA and Blocks the Inhibitory Effects of Molecular Markers of Alzheimer’s Disease on the Pump Activity

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