A novel serine/threonine kinase gene, STK33 , on human chromosome 11p15.3

Mujica, Alejandro O.; Hankeln, Thomas; Schmidt, Erwin R.

doi:10.1016/s0378-1119(01)00780-6

Cited by 35 publications

(33 citation statements)

References 25 publications

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“…The human serine/threonine kinase 33 (STK33) gene (called stk33 in mouse) is located on chromosome 11, region 11p15.3, and includes 12 introns and a 1545 bp open-reading frame; while the stk33 gene is found on chromosome 7 in mouse [1,2]. Researchers have analyzed STK33 mRNA and protein expression in many normal human adult and embryonic tissues to investigate the distribution and location of STK33.…”

Section: Introductionmentioning

confidence: 99%

STK33 plays an important positive role in the development of human large cell lung cancers with variable metastatic potential

Wang¹,

Cheng²,

Wu³

et al. 2015

ABBS

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Serine/threonine kinase 33 (STK33) is a novel protein that has attracted considerable interest in recent years. Previous research has revealed that STK33 expression plays a special role in cancer cell proliferation. However, the mechanisms of STK33 induction of cancer cells remain largely unknown. In this study, it is demonstrated that STK33 expression varies in NL9980 and L9981 cells which are homogeneous cell lines with similar genetic backgrounds. STK33 can promote cell migration and invasion and suppress p53 gene expression in the NL9980 and L9981 cells. In addition, this protein also promotes epithelial-mesenchymal transition (EMT). Moreover, STK33 knockdown decreases tumor-related gene expression and inhibits cell migration, invasion, and EMT, suggesting that STK33 may be a mediator of signaling pathways that are involved in cancer. In conclusion, our results suggest that STK33 may be an important prognostic marker and a therapeutic target for the metastatic progression of human lung cancer.

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Section: Introductionmentioning

confidence: 99%

STK33 plays an important positive role in the development of human large cell lung cancers with variable metastatic potential

Wang¹,

Cheng²,

Wu³

et al. 2015

ABBS

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“…In one of these studies, STK33, a poorly characterized kinase, was identified as a candidate drug target for mutant KRAS tumors (3). STK33 is a serine-threonine kinase that belongs to the calcium/calmodulin-dependent family of kinases (4). The physiologic function of STK33 is unknown and STK33 does not seem to be genetically altered in cancers (3).…”

Section: Introductionmentioning

confidence: 99%

STK33 Kinase Activity Is Nonessential in KRAS-Dependent Cancer Cells

et al. 2011

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Despite the prevalence of KRAS mutations in human cancers, there remain no targeted therapies for treatment. The serine-threonine kinase STK33 has been proposed to be required for the survival of mutant KRAS-dependent cell lines, suggesting that small molecule kinase inhibitors of STK33 may be useful to treat KRAS-dependent tumors. In this study, we investigated the role of STK33 in mutant KRAS human cancer cells using RNA interference, dominant mutant overexpression, and small molecule inhibitors. As expected, KRAS downregulation decreased the survival of KRAS-dependent cells. In contrast, STK33 downregulation or dominant mutant overexpression had no effect on KRAS signaling or survival of these cells. Similarly, a synthetic lethal siRNA screen conducted in a broad panel of KRAS wild-type or mutant cells identified KRAS but not STK33 as essential for survival. We also obtained similar negative results using small molecule inhibitors of the STK33 kinase identified by high-throughput screening. Taken together, our findings refute earlier proposals that STK33 inhibition may be a useful therapeutic approach to target human KRAS mutant tumors. Cancer Res; 71(17); 5818-26. Ó2011 AACR.

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“…It is a serine/threonine kinase and member of the Ca 2+ /calmodulin-dependent kinase family. 53 STK33 autophosphorylates and interacts with and phosphorylates Vimentin. Vimentin, an intermediate filament protein, reportedly interacts with HIV-1 Vif, 54 is cleaved by HIV-protease, 55 and its phosphorylation can be inhibited by the HIV-1 envelope protein, gp120.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Early HIV-1 Nucleoprotein Complexes

et al. 2013

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After entry into the cell, the early steps of the human immunodeficiency virus type 1 (HIV-1) replication cycle are mediated by two functionally distinct nucleoprotein complexes, the reverse transcription complex (RTC) and preintegration complex (PIC). These two unique viral complexes are responsible for the conversion of the single-stranded RNA genome into double stranded DNA, transport of the DNA into the nucleus, and integration of the viral DNA into the host cell chromosome. Prior biochemical analyses suggest that these complexes are large and contain multiple undiscovered host cell factors. In this study functional HIV-1 RTCs and PICs were partially purified by velocity gradient centrifugation and fractionation, concentrated, trypsin digested, and analyzed by LC-MS/MS. A total of seven parallel infected and control biological replicates were completed. Database searches were performed with Proteome Discoverer and a comparison of the HIV-1 samples to parallel uninfected control samples was used to identify unique cellular factors. The analysis produced a total data set of 11,055 proteins. Several previously characterized HIV-1 factors were identified, including XRCC6, TFRC, and HSP70. The presence of XRCC6 was confirmed in infected fractions, and shown to be associated with HIV-1 DNA by immunoprecipitation-PCR experiments. Overall, the analysis identified 94 proteins unique in the infected fractions and 121 proteins unique to the control fractions with ≥ 2 protein assignments. An additional 54 and 52 were classified as enriched in the infected and control samples, respectively, based on a three-fold difference in total Proteome Discoverer probability score. The differential expression of several candidate proteins was validated by Western blot analysis. This study contributes additional novel candidate proteins to the growing published bioinformatic data sets of proteins that contribute to HIV-1 replication.

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A novel serine/threonine kinase gene, STK33 , on human chromosome 11p15.3

Cited by 35 publications

References 25 publications

STK33 plays an important positive role in the development of human large cell lung cancers with variable metastatic potential

STK33 plays an important positive role in the development of human large cell lung cancers with variable metastatic potential

STK33 Kinase Activity Is Nonessential in KRAS-Dependent Cancer Cells

Proteomic Analysis of Early HIV-1 Nucleoprotein Complexes

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