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Sharma, A. L.

Publications and source records attributed to Sharma, A. L..

3 recordsLinked to original sources

HIV and Cocaine exposure promote Tau phosphorylation through RSK-1 in a GSK3β-independent manner.

HIV and cocaine are known to disrupt neuronal signaling and contribute to neurocognitive dysfunction, yet the underlying molecular mechanisms are not clear. In this study, we delineate the underlying molecular mechanism by which HIV and/or cocaine enhance Tau phosphorylation (p-Tau S396), a marker of Tau-mediated neuropathies. Furthermore, we elucidate how these two independent neuropathogenic factors, cocaine and HIV, exploit distinct yet convergent signaling pathways to drive this pathological event. We demonstrate that HIV robustly activates and upregulates RSK1, which functions upstream of AKT and promotes Tau phosphorylation through an AKT-independent mechanism while simultaneously inactivating GSK3{beta} via serine-9 phosphorylation (p-GSK3{beta} S9). However, cocaine not only activates RSK1 but also strongly stimulates AKT1, resulting in sustained GSK3{beta} inhibition and persistent Tau phosphorylation. Notably, Tau phosphorylation persists even under conditions of GSK3{beta} inactivation in both HIV and cocaine exposure, revealing a previously unrecognized GSK3{beta}-independent mechanism of Tau modification. Collectively, these findings identify RSK1 as the primary mediator of Tau phosphorylation upon HIV and/or cocaine exposure, and uncover a novel RSK1-driven, GSK3{beta}-independent pathway contributing to Tauopathy. Through a combination of immunofluorescence, immunoblotting, genetic knockout, and overexpression approaches, we establish RSK1 as a central signaling hub linking the AKT-GSK3{beta} pathway to Tau phosphorylation. We demonstrate that RSK1 operates as a critical upstream regulator of AKT and GSK3{beta} signaling, playing dual roles, both activating AKT and suppressing GSK3{beta}, thereby uncovering a novel layer of pathways that regulates Tau phosphorylation. The reproducibility of these main signaling pathways across SH-SY5Y neurons, mixed cell 3D spheroids, and human brain organoids underscores the robustness and biological relevance of this mechanism. Collectively, these findings reveal mechanistic convergence of HIV and cocaine on RSK1-dependent signaling and provide critical insight into how diverse neuropathic / neuropathological factors remodel neuronal signaling to drive Tau-associated dysfunction. These findings provide novel mechanistic insight into the molecular underpinnings of neuro-HIV and substance abuse associated Tauopathy. By identifying RSK1 as a master regulator and demonstrating that Tau phosphorylation can bypass GSK3{beta} inhibition, our study advances understanding of signaling complexity and highlights new opportunities for therapeutic intervention. Targeting RSK1 may represent a promising strategy to mitigate Tau pathology, induced due to insoluble aggregates of phosphorylated Tau, a common factor promoting cognitive decline not only in individuals with Alzheimers disease but also in those exposed to cocaine or/and infected with HIV. SignificancesThis study demonstrates that exposure to HIV and/or cocaine induces Tau phosphorylation at serine 396 (S396), a well-established marker of Tau pathology, and delineates how these two independent neuropathogenic factors engage distinct yet convergent signaling pathways to drive this pathogenic event. We show that HIV exposure drives robust RSK1 activation, positioning it upstream of AKT to promote Tau phosphorylation via an AKT-independent mechanism, while concurrently suppressing GSK3{beta} activity through serine-9 phosphorylation. In contrast, cocaine, while only moderately activating RSK1, primarily enhances AKT signaling, leading to sustained GSK3{beta} inhibition and increased Tau phosphorylation. Notably, Tau phosphorylation persists even under conditions of GSK3{beta} inactivation in both settings, revealing a previously unrecognized, RSK1-centered, GSK3{beta}-independent pathway of Tau modification. Overall, our findings demonstrate that Tau phosphorylation in the context of HIV infection and cocaine exposure is a complex, multi-layered regulatory process involving multiple signaling nodes. Importantly, we identify RSK1 as a central integrative hub linking viral and substance-induced signaling to downstream Tau pathology. This work advances our understanding of the molecular mechanisms underlying neuroHIV and substance abuse-associated neurodegeneration. Furthermore, it highlights RSK1 as a novel and promising therapeutic target for mitigating Tauopathy in both cocaine-using and non-using people with HIV (PWH). Highlighted pointsO_LIRSK1 acts as a central regulator of Tau phosphorylation, capable of driving this process through a GSK3{beta}-independent mechanism. C_LIO_LIHIV promotes Tau phosphorylation primarily via robust upregulation and activation of RSK1, operating largely independent of AKT1, while concurrently inducing GSK3{beta} inactivation. C_LIO_LIDrugs of abuse, such as cocaine induces Tau phosphorylation through dual activation of AKT1 and RSK1, alongside sustained inactivation of GSK3{beta}. C_LIO_LITau phosphorylation persists despite GSK3{beta} inhibition, revealing a complex AKT1-RSK1 signaling axis and underscoring the dominant role of GSK3{beta}-independent mechanisms in Tau pathology following HIV and cocaine exposure. C_LIO_LIHIV and cocaine engage distinct yet convergent signaling pathways that disrupt neuronal homeostasis and drive tauopathy, providing mechanistic insight into neuroHIV and substance abuse-associated neurodegeneration. C_LIO_LIRSK1 functions as a key upstream modulator of AKT and GSK3{beta} pathways, positively regulating AKT signaling while negatively regulating GSK3{beta} activity. C_LIO_LIRSK1 emerges as a potential therapeutic target, offering new opportunities for intervention in HIV-associated neurocognitive disorders (HAND) and drug-induced neurodegeneration. C_LIO_LIEstablished and characterized H80 cells as a novel neuronal cell model and demonstrated their suitability for studying neuron-specific signaling pathways, including Tau phosphorylation. C_LIO_LIThe conserved and widespread nature of the signaling cascade driving Tau phosphorylation in response to HIV and/or cocaine exposure was validated across multiple model systems, including both 2D neuronal cell cultures and 3D systems such as human brain organoids and spheroids. C_LI Strength of the StudyThis original study provides novel mechanistic insight into how HIV and cocaine, two independent neuropathological factors, converge and diverge on intracellular signaling pathways to regulate Tau phosphorylation. By integrating immunofluorescence, immunoblotting, genetic knockout, and overexpression approaches, we identified RSK1 as a master regulator of Tau phosphorylation. Importantly, we discovered that HIV robustly upregulates and activates RSK1 to promote Tau phosphorylation through an AKT-independent route while simultaneously inactivating GSK3{beta}. On the other hand, cocaine exerts a moderate effect on RSK1 but strongly stimulates AKT to induce GSK3{beta} inactivation and drive Tau phosphorylation. A key strength of this work is the discovery that Tau phosphorylation persists despite GSK3{beta} inactivation, revealing a complex, GSK3{beta}-independent mechanism, involving RSK1 in Tau pathology. Moreover, our study, for the first time, identify RSK1 as an upstream regulator of AKT-GSK3{beta} signaling cascade, enhancing AKT signaling while simultaneously inhibiting GSK3{beta} activity, thereby underscoring the critical role of RSK1 in Tau phosphorylation and associated illnesses, such as HAND and Alzheimers disease. Together, these findings not only advance our understanding of the molecular underpinnings of neuroHIV and substance abuse associated tauopathy but also highlight RSK1 as a promising therapeutic target for not only HIV and cocaine induced neurotoxicity but also other neurodegenerative diseases, such as Alzheimers disease. Another key strength of this study is the establishment and characterization of H80 cells as a novel neuronal model, demonstrating their suitability for investigating neuron-specific signaling pathways, including Tau phosphorylation. The combination of comparative signaling analysis, genetic perturbations, and integrative mechanistic modeling makes this study both conceptually and technically novel, besides broadly relevant to the fields of neurovirology, addiction neuroscience, neurodegeneration, and cognitive impairments.

molecular biology↗

Cocaine-induced DNA-PK relieves RNAP II pausing by promoting TRIM28 phosphorylation.

Drug abuse continues to pose a significant challenge in HIV control efforts. In our investigation, we discovered that cocaine not only upregulates the expression of DNA-dependent protein kinase (DNA-PK) but also augments DNA-PK activation by enhancing its phosphorylation at S2056. Moreover, DNA-PK phosphorylation triggers the translocation of DNA-PK into the nucleus. The finding that cocaine promotes nuclear translocation of DNA-PK further validates our observation of enhanced DNA-PK recruitment at the HIV long terminal repeat (LTR) following cocaine exposure. By activating and facilitating the nuclear translocation of DNA-PK, cocaine effectively orchestrates multiple stages of HIV transcription, thereby promoting HIV replication. Additionally, our study indicates that cocaine-induced DNA-PK promotes hyper-phosphorylation of RNA polymerase II (RNAP II) carboxyl-terminal domain (CTD) at Ser5 and Ser2 sites, enhancing both initiation and elongation phases, respectively, of HIV transcription. Cocaines enhancement of transcription initiation and elongation is further supported by its activation of cyclin-dependent kinase 7 (CDK7) and subsequent phosphorylation of CDK9, thereby promoting positive transcriptional elongation factor b (P-TEFb) activity. We demonstrate for the first time that cocaine, through DNA-PK activation, promotes the specific phosphorylation of TRIM28 at Serine 824 (p-TRIM28, S824). This modification converts TRIM28 from a transcriptional inhibitor to a transactivator for HIV transcription. Additionally, we observe that phosphorylation of TRIM28 (p-TRIM28, S824) promotes the transition from the pausing phase to the elongation phase of HIV transcription, thereby facilitating the production of full-length HIV genomic transcripts. This finding corroborates the observed enhanced RNAP II CTD phosphorylation at Ser2, a marker of transcriptional elongation, following cocaine exposure. Accordingly, upon cocaine treatment, we observed elevated recruitment of p-TRIM28-(S824) at the HIV LTR. Overall, our results have unraveled the intricate molecular mechanisms underlying cocaine-induced HIV transcription and gene expression. These findings hold promise for the development of highly targeted therapeutics aimed at mitigating the detrimental effects of cocaine in individuals living with HIV. Highlights of the studyO_LICocaine upregulates both the expression and activity of DNA-PK. C_LIO_LICocaine augments the phosphorylation of DNA-PK selectively at S2056, a post-translational modification that marks functionally active form of DNA-PK. C_LIO_LICocaine enhances the nuclear translocation of DNA-PK. C_LIO_LIThe DNA-PK inhibition severely impairs HIV transcription, replication, and latency reactivation. C_LIO_LICocaine facilitates the initiation and elongation phases of HIV by enhancing RNAPII CTD phosphorylation at Ser5 and Ser2, respectively, by stimulating DNA-PK. C_LIO_LICocaine also supports initiation and elongation phases of HIV transcription by stimulating CDK7 (the kinase of TFIIH) and CDK9 (the kinase subunit of P-TEFb), respectively. C_LIO_LICocaine-mediated activation of DNA-PK relieves RNAP II pausing by reversing the inhibitory effect of pausing factor TRIM28 and converting it into a transactivator by catalyzing its phosphorylation at S824 site. C_LIO_LIThus, cocaine, by activating DNA-PK, facilitates the multiple phases of HIV transcription, namely, initiation, RNAP II pause-release, and elongation. C_LI

molecular biology↗

Ovarian cancer G protein-coupled receptor 1 inhibits A549 cells Migration through Casein kinase 2α intronless gene and Neutral endopeptidase

We have previously reported that ovarian cancer G protein-coupled receptor 1 (OGR1) is a new metastasis suppressor gene. We have also reported for the first time that a new intronless gene for casein kinase 2 (CSNK2A3) is expressed in human cells. The promoter of the well-known casein kinase 2 (CSNK2A1) displays characteristics of housekeeping gene whereas CSNK2A3 has a characteristic of a regulated promoter with two TATA boxes and a CAAT box. In this study, we found that OGR1 up-regulates expression of CSNK2A3 by about 3 folds in A549 cells but not CSNK2A1. OGR1 also up-regulates expression of neutral endopeptidase (NEP). The OGR1 induced inhibition of A549 cell migration is completely abrogated by inhibition of casein kinase 2 activity, whereas partial abrogation (~ 30%) was observed in the presence of NEP inhibition. The results also revealed that OGR1 regulates CSNK2A3 via activation of Rac1/cdc42 and MAPKs pathways. CK2 is ubiquitously expressed and in contrast it is believed to be a constitutively active enzyme and its regulation appears to be independent of known second messengers. There is no previous report on how expression of CK2 in cancer cells is regulated although many studies have report of aberrant expression of the kinase in cancer. In the current study, we are reporting for the first time the regulation of intronless casein kinase 2 gene, CSNK2A3 in cancer cells. Our findings suggest that the aberrantly casein kinase 2 expression found in various cancer cells may the due to CSNK2A3 expression which is potentially regulated by several master regulators of the developmental pathways rather than well-known casein kinase 2 gene, CSNK2A1.

cancer biology↗