RETRACTED: PAK5 facilitates the proliferation, invasion and migration in colorectal cancer cells

Huang, Silin; Zhu, Ying; Wang, Chunfei; Li, Xiaxi; Cui, Xiaobing; Tu, Sufang; You, Lijuan; Fu, Jingwen; Chen, Zemin; Hu, Wei; Gong, Wei

doi:10.1002/cam4.3084

Cited by 14 publications

(8 citation statements)

References 53 publications

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“…15 Recently, some scholars have implicated the role of PAK7 in the pathology of malignant tumors. For instance, PAK7 was upregulated in the human colorectal cancer, showing an association with its tumor progression and metastasis, as suggested by Huang et al 16 In lung squamous cell carcinoma, PAK7 was also highly expressed and knockout of PAK7 could inhibit the growth and metastasis of its tumor cells. 17 Importantly, PAK7 demonstrated a similar expression pattern as the above in HCC.…”

Section: Introductionmentioning

confidence: 75%

Inhibiting p21-activated kinase (PAK7) enhances radiosensitivity in hepatocellular carcinoma

2021

Hum Exp Toxicol

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Objective: In light of the upregulation of p21-activated kinase (PAK7) in a variety of cancers, including hepatocellular carcinoma (HCC), we aimed to investigate the effect of PAK7 on the sensitivity of HCC cells to radiotherapy. Methods: PAK7 expression was determined in normal adult liver epithelial THLE-2 and human HCC cell lines. The effect of ionizing radiation (IR) on the HCC cell viability was evaluated by Sulforhodamine B (SRB) assay. HCC cell lines Mahlavu and Huh7 were chosen to assess the effect of PAK7 shRNAs on the viability, clone formation, apoptosis, cycle distribution and γ-H2AX expression after exposure to IR. Results: As compared to THLE-2 cells, PAK7 was upregulated in poorly differentiated Mahlavu and SK-Hep-1 cells, but moderately or lowly expressed in well-differentiated Huh7 and HepG2 cells. HCC cells with moderate or low expression of PAK7 presented a decreased viability at 2 Gy IR, which had no significant effect on PAK7high HCC cells. Mahlavu and Huh7 cells transfected with PAK7 shRNAs showed increased inhibitory effect of IR on viability. In addition, PAK7 shRNAs reduced clone formation, facilitated the cell apoptosis, arrested cells at G2/M phase, and increased γ-H2AX expression. Moreover, changes above were more evident in the HCC cells co-treated with IR and PAK7 shRNAs. Conclusion: PAK7 downregulation could inhibit the viability, promote the apoptosis, arrest cells in G2/M phase, and induce the DNA damage in HCC cells, thereby enhancing the radiosensitivity in HCC.

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Section: Introductionmentioning

confidence: 75%

Inhibiting p21-activated kinase (PAK7) enhances radiosensitivity in hepatocellular carcinoma

2021

Hum Exp Toxicol

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“…In contrast, PAK5, CDK17, and NEK6 belong to the group of understudied, less well‐characterized kinases. PAK5 (formerly PAK7) is an actin‐ and microtubule‐associated, p21 cdc42/rac1 ‐activated kinase family member (Cau et al , 2001), which has been shown to promote proliferation, invasion, and migration of various cancer cell models (Huang et al , 2020). CDK17 (also PCTAIRE2) is an uncharacterized member of the cyclin‐dependent kinase family (Malumbres et al , 2009).…”

Section: Discussionmentioning

confidence: 99%

A human kinase yeast array for the identification of kinases modulating phosphorylation‐dependent protein–protein interactions

Jehle

Kunowska

Benlasfer

et al. 2022

Molecular Systems Biology

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Protein kinases play an important role in cellular signaling pathways and their dysregulation leads to multiple diseases, making kinases prime drug targets. While more than 500 human protein kinases are known to collectively mediate phosphorylation of over 290,000 S/T/Y sites, the activities have been characterized only for a minor, intensively studied subset. To systematically address this discrepancy, we developed a human kinase array in Saccharomyces cerevisiae as a simple readout tool to systematically assess kinase activities. For this array, we expressed 266 human kinases in four different S. cerevisiae strains and profiled ectopic growth as a proxy for kinase activity across 33 conditions. More than half of the kinases showed an activity‐dependent phenotype across many conditions and in more than one strain. We then employed the kinase array to identify the kinase(s) that can modulate protein–protein interactions (PPIs). Two characterized, phosphorylation‐dependent PPIs with unknown kinase–substrate relationships were analyzed in a phospho‐yeast two‐hybrid assay. CK2α1 and SGK2 kinases can abrogate the interaction between the spliceosomal proteins AAR2 and PRPF8, and NEK6 kinase was found to mediate the estrogen receptor (ERα) interaction with 14‐3‐3 proteins. The human kinase yeast array can thus be used for a variety of kinase activity‐dependent readouts.

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“…In contrast, PAK5, CDK17 and NEK6 belong to the group of understudied, less well characterized kinases. PAK5 (formerly PAK7) is an actin and microtubule associated p21 cdc42/rac1 -activated kinase family member [73], which has been shown to promote proliferation, invasion and migration of various cancer cell models [74]. CDK17 (also PCTAIRE2) is an uncharacterized member of the cyclin-dependent kinase family [75].…”

Section: Discussionmentioning

confidence: 99%

A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactions

Jehle

Kunowska

Benlasfer

et al. 2021

Preprint

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Protein kinases play an important role in cellular signaling pathways and their dysregulation leads to multiple diseases, making kinases prime drug targets. While more than 500 human protein kinases are known to collectively mediate phosphorylation of over 290,000 S/T/Y sites, the activities have been characterized only for a minor, intensively studied subset. To systematically address this discrepancy, we developed a human kinase array in Saccharomyces cerevisiae as a simple readout tool to systematically assess kinase activities. For this array, we expressed 266 human kinases in four different Saccharomyces cerevisiae strains and profiled ectopic growth as a proxy for kinase activity across 33 conditions. More than half of the kinases showed an activity-dependent phenotype across many conditions and in more than one strain. We then employed the kinase array to identify the kinase(s) that can modulate protein-protein-interactions (PPIs). Two characterized, phosphorylation-dependent PPIs with unknown kinase-substrate relationships were analyzed in a phospho-yeast two-hybrid assay. CK2α1 and SGK2 kinases can abrogate the interaction between the spliceosomal proteins AAR2 and PRPF8 and NEK6 kinase was found to mediate the estrogen receptor (ERα) interaction with 14-3-3 proteins. The human kinase yeast array can thus be used for a variety of kinase activity-dependent readouts.

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RETRACTED: PAK5 facilitates the proliferation, invasion and migration in colorectal cancer cells

Cited by 14 publications

References 53 publications

Inhibiting p21-activated kinase (PAK7) enhances radiosensitivity in hepatocellular carcinoma

Inhibiting p21-activated kinase (PAK7) enhances radiosensitivity in hepatocellular carcinoma

A human kinase yeast array for the identification of kinases modulating phosphorylation‐dependent protein–protein interactions

A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactions

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