2019
DOI: 10.18632/oncotarget.27282
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Correction: Protein 4.1N acts as a potential tumor suppressor linking PP1 to JNK-c-Jun pathway regulation in NSCLC

Abstract: This article has been corrected: During the assembly of Figure 2B, the same image was inadvertently used for both H1299 (pEGFP-C3) and H1299 (pEGFP-4.1N) groups at 0h time point. The proper Figure 2 B specific for H1299 (pEGFP-C3) and H1299 (pEGFP-4.1N) groups are shown below. The authors declare that these corrections do not change the results or conclusions of this paper.

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“…Ji et al showed that protein 4.1N is differentially expressed in cell lines with different metastatic abilities and is not expressed in breast cancer cell lines with high metastatic properties, revealing the vital role that protein 4.1N plays in breast cancer metastasis and revealing that protein 4.1N is a negative regulator affecting cancer cell adhesion, migration, and invasion [ 53 ]. Wang et al showed that the expression level of protein 4.1N was negatively correlated with the metastatic ability of small cell lung cancer cell lines and that low expression of protein 4.1N promoted the progression of non-small cell lung cancer [ 54 ]. The FERM domain of protein 4.1N, which is required for its localization and stabilization in the basement membrane, binds to protein phosphatase1 (PP1), and PP1-mediated dephosphorylation contributes to the localization of protein 4.1N.…”
Section: Function Of Cytoskeleton Protein 41mentioning
confidence: 99%
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“…Ji et al showed that protein 4.1N is differentially expressed in cell lines with different metastatic abilities and is not expressed in breast cancer cell lines with high metastatic properties, revealing the vital role that protein 4.1N plays in breast cancer metastasis and revealing that protein 4.1N is a negative regulator affecting cancer cell adhesion, migration, and invasion [ 53 ]. Wang et al showed that the expression level of protein 4.1N was negatively correlated with the metastatic ability of small cell lung cancer cell lines and that low expression of protein 4.1N promoted the progression of non-small cell lung cancer [ 54 ]. The FERM domain of protein 4.1N, which is required for its localization and stabilization in the basement membrane, binds to protein phosphatase1 (PP1), and PP1-mediated dephosphorylation contributes to the localization of protein 4.1N.…”
Section: Function Of Cytoskeleton Protein 41mentioning
confidence: 99%
“…Protein 4.1N can recruit PP1 to affect the processes of adhesion and proliferation in non-small cell lung cancer by inhibiting critical molecules of the JNK-c-Jun pathway. In microcarcinoma, the CTD structural domain of protein 4.1N can bind to the N-terminal end of Pike, an enhancer of PI3K, and the competitive binding effect of the two leads to cell cycle alterations, which in turn affects the progression of cancer [ 54 ].…”
Section: Function Of Cytoskeleton Protein 41mentioning
confidence: 99%