Journal of signal transduction最新文献_第5页

The Small GTPase Rap1b: A Bidirectional Regulator of Platelet Adhesion Receptors. 小GTPase Rap1b:血小板粘附受体的双向调节剂。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2012-06-14 DOI: 10.1155/2012/412089

Gianni Francesco Guidetti, Mauro Torti

引用次数: 40

Dopamine D(2) Receptor-Mediated Heterologous Sensitization of AC5 Requires Signalosome Assembly. 多巴胺D(2)受体介导的AC5异源致敏需要信号体组装。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2012-03-12 DOI: 10.1155/2012/210324

Karin F K Ejendal, Carmen W Dessauer, Terence E Hébert, Val J Watts

引用次数: 7

A Bioinformatics Resource for TWEAK-Fn14 Signaling Pathway. TWEAK-Fn14信号通路的生物信息学资源。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2012-05-09 DOI: 10.1155/2012/376470

Mitali Bhattacharjee, Rajesh Raju, Aneesha Radhakrishnan, Vishalakshi Nanjappa, Babylakshmi Muthusamy, Kamlendra Singh, Dheebika Kuppusamy, Bhavya Teja Lingala, Archana Pan, Premendu Prakash Mathur, H C Harsha, T S Keshava Prasad, Gerald J Atkins, Akhilesh Pandey, Aditi Chatterjee

{"title":"A Bioinformatics Resource for TWEAK-Fn14 Signaling Pathway.","authors":"Mitali Bhattacharjee, Rajesh Raju, Aneesha Radhakrishnan, Vishalakshi Nanjappa, Babylakshmi Muthusamy, Kamlendra Singh, Dheebika Kuppusamy, Bhavya Teja Lingala, Archana Pan, Premendu Prakash Mathur, H C Harsha, T S Keshava Prasad, Gerald J Atkins, Akhilesh Pandey, Aditi Chatterjee","doi":"10.1155/2012/376470","DOIUrl":"https://doi.org/10.1155/2012/376470","url":null,"abstract":"TNF-related weak inducer of apoptosis (TWEAK) is a new member of the TNF superfamily. It signals through TNFRSF12A, commonly known as Fn14. The TWEAK-Fn14 interaction regulates cellular activities including proliferation, migration, differentiation, apoptosis, angiogenesis, tissue remodeling and inflammation. Although TWEAK has been reported to be associated with autoimmune diseases, cancers, stroke, and kidney-related disorders, the downstream molecular events of TWEAK-Fn14 signaling are yet not available in any signaling pathway repository. In this paper, we manually compiled from the literature, in particular those reported in human systems, the downstream reactions stimulated by TWEAK-Fn14 interactions. Our manual amassment of the TWEAK-Fn14 pathway has resulted in cataloging of 46 proteins involved in various biochemical reactions and TWEAK-Fn14 induced expression of 28 genes. We have enabled the availability of data in various standard exchange formats from NetPath, a repository for signaling pathways. We believe that this composite molecular interaction pathway will enable identification of new signaling components in TWEAK signaling pathway. This in turn may lead to the identification of potential therapeutic targets in TWEAK-associated disorders.","PeriodicalId":89176,"journal":{"name":"Journal of signal transduction","volume":"2012 ","pages":"376470"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/376470","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30656336","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 31

ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-X-X-Cys Redox Centres and Iron-Based Oxidative Stress. 细菌中ros介导的信号传导:含锌Cys-X-X-Cys氧化还原中心和铁基氧化应激。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2011-09-29 DOI: 10.1155/2012/605905

Darío Ortiz de Orué Lucana, Ina Wedderhoff, Matthew R Groves

{"title":"ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-X-X-Cys Redox Centres and Iron-Based Oxidative Stress.","authors":"Darío Ortiz de Orué Lucana, Ina Wedderhoff, Matthew R Groves","doi":"10.1155/2012/605905","DOIUrl":"https://doi.org/10.1155/2012/605905","url":null,"abstract":"Bacteria are permanently in contact with reactive oxygen species (ROS), both over the course of their life cycle as well that present in their environment. These species cause damage to proteins, lipids, and nucleotides, negatively impacting the organism. To detect these ROS molecules and to stimulate the expression of proteins involved in antioxidative stress response, bacteria use a number of different protein-based regulatory and sensory systems. ROS-based stress detection mechanisms induce posttranslational modifications, resulting in overall conformational and structural changes within sensory proteins. The subsequent structural rearrangements result in changes of protein activity, which lead to regulated and appropriate response on the transcriptional level. Many bacterial enzymes and regulatory proteins possess a conserved signature, the zinc-containing redox centre Cys-X-X-Cys in which a disulfide bridge is formed upon oxidative stress. Other metal-dependent oxidative modifications of amino acid side-chains (dityrosines, 2-oxo-histidines, or carbonylation) also modulate the activity of redox-sensitive proteins. Using molecular biology, biochemistry, biophysical, and structure biology tools, molecular mechanisms involved in sensing and response to oxidative stress have been elucidated in detail. In this review, we analyze some examples of bacterial redox-sensing proteins involved in antioxidative stress response and focus further on the currently known molecular mechanism of function.","PeriodicalId":89176,"journal":{"name":"Journal of signal transduction","volume":"2012 ","pages":"605905"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/605905","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30188436","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 70

Redox Regulation of Nonmuscle Myosin Heavy Chain during Integrin Engagement. 整合素参与过程中非肌球蛋白重链的氧化还原调控。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2011-12-19 DOI: 10.1155/2012/754964

Tania Fiaschi, Giacomo Cozzi, Paola Chiarugi

{"title":"Redox Regulation of Nonmuscle Myosin Heavy Chain during Integrin Engagement.","authors":"Tania Fiaschi, Giacomo Cozzi, Paola Chiarugi","doi":"10.1155/2012/754964","DOIUrl":"https://doi.org/10.1155/2012/754964","url":null,"abstract":"On the basis of our findings reporting that cell adhesion induces the generation of reactive oxygen species (ROS) after integrin engagement, we were interested in identifying redox-regulated proteins during this process. Mass spectrometry analysis led us to identify nonmuscle myosin heavy chain (nmMHC) as a target of ROS. Our results show that, while nmMHC is reduced in detached/rounded cells, it turns towards an oxidized state in adherent/spread cells due to the integrin-engaged ROS machinery. The functional role of nmMHC redox regulation is suggested by the redox sensitivity of its association with actin, suggesting a role of nmMHC oxidation in cytoskeleton movement. Analysis of muscle MHC (mMHC) redox state during muscle differentiation, a process linked to a great and stable decrease of ROS content, shows that the protein does not undergo a redox control. Hence, we propose that the redox regulation of MHC in nonprofessional muscle cells is mandatory for actin binding during dynamic cytoskeleton rearrangement, but it is dispensable for static and highly organized cytoskeletal contractile architecture in differentiating myotubes.","PeriodicalId":89176,"journal":{"name":"Journal of signal transduction","volume":"2012 ","pages":"754964"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/754964","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30365677","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 11

Extracellular Signal-Regulated Kinase (ERK) Activation and Mitogen-Activated Protein Kinase Phosphatase 1 Induction by Pulsatile Gonadotropin-Releasing Hormone in Pituitary Gonadotrophs. 垂体促性腺激素释放激素对细胞外信号调节激酶(ERK)激活和丝裂原活化蛋白激酶磷酸酶1的诱导作用。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2011-12-22 DOI: 10.1155/2012/198527

Haruhiko Kanasaki, Indri Purwana, Aki Oride, Tselmeg Mijiddorj, Kohji Miyazaki

{"title":"Extracellular Signal-Regulated Kinase (ERK) Activation and Mitogen-Activated Protein Kinase Phosphatase 1 Induction by Pulsatile Gonadotropin-Releasing Hormone in Pituitary Gonadotrophs.","authors":"Haruhiko Kanasaki, Indri Purwana, Aki Oride, Tselmeg Mijiddorj, Kohji Miyazaki","doi":"10.1155/2012/198527","DOIUrl":"https://doi.org/10.1155/2012/198527","url":null,"abstract":"The frequency of gonadotropin-releasing hormone (GnRH) pulse secreted from the hypothalamus differently regulates the expressions of gonadotropin subunit genes, luteinizing hormone β (LHβ) and follicle-stimulating hormone β (FSHβ), in the pituitary gonadotrophs. FSHβ is preferentially stimulated at slower GnRH pulse frequencies, whereas LHβ is preferentially stimulated at more rapid pulse frequencies. Several signaling pathways are activated, including mitogen-activated protein kinase (MAPK), protein kinase C, calcium influx, and calcium-calmodulin kinases, and these may be preferentially regulated under certain conditions. Previous studies demonstrated that MAPK pathways, especially the extracellular signal-regulated kinase (ERK), play an essential role for induction of gonadotropin subunit gene expression by GnRH, whereas, MAPK phosphatases (MKPs) inactivate MAPKs through dephosphorylation of threonine and/or tyrosine residues. MKPs are also induced by GnRH, and potential feedback regulation between MAPK signaling and MKPs within the GnRH signaling pathway is evident in gonadotrophs. In this paper, we reviewed and mainly focused on our observations of the pattern of ERK activation and the induction of MKP by different frequencies of GnRH stimulation.","PeriodicalId":89176,"journal":{"name":"Journal of signal transduction","volume":"2012 ","pages":"198527"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/198527","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30378197","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 12

Molecular Crosstalk between Integrins and Cadherins: Do Reactive Oxygen Species Set the Talk? 整合素和钙粘蛋白之间的分子串扰:活性氧是否起主导作用?

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2011-12-13 DOI: 10.1155/2012/807682

Luca Goitre, Barbara Pergolizzi, Elisa Ferro, Lorenza Trabalzini, Saverio Francesco Retta

引用次数: 55

Elimination of the actin-binding domain in kelch-like 1 protein induces T-type calcium channel modulation only in the presence of action potential waveforms. kelch样1蛋白中肌动蛋白结合域的消除仅在动作电位波形存在的情况下诱导t型钙通道调节。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2012-07-11 DOI: 10.1155/2012/505346

Kelly A Aromolaran, Kelly A Benzow, Leanne L Cribbs, Michael D Koob, Erika S Piedras-Rentería

{"title":"Elimination of the actin-binding domain in kelch-like 1 protein induces T-type calcium channel modulation only in the presence of action potential waveforms.","authors":"Kelly A Aromolaran, Kelly A Benzow, Leanne L Cribbs, Michael D Koob, Erika S Piedras-Rentería","doi":"10.1155/2012/505346","DOIUrl":"https://doi.org/10.1155/2012/505346","url":null,"abstract":"The Kelch-like 1 protein (KLHL1) is a neuronal actin-binding protein that modulates calcium channel function. It increases the current density of Ca(v)3.2 (α(1H)) calcium channels via direct interaction with α(1H) and actin-F, resulting in biophysical changes in Ca(v)3.2 currents and an increase in recycling endosomal activity with subsequent increased α(1H) channel number at the plasma membrane. Interestingly, removal of the actin-binding Kelch motif (ΔKelch) prevents the increase in Ca(v)3.2 current density seen with wild-type KLHL1 when tested with normal square pulse protocols but does not preclude the effect when tested using action potential waveforms (AP). Here, we dissected the kinetic properties of the AP waveform that confer the mutant Kelch the ability to interact with Ca(v)3.2 and induce an increase in calcium influx. We modified the action potential waveform by altering the slopes of repolarization and/or recovery from hyperpolarization or by changing the duration of the depolarization plateau or the hyperpolarization phase and tested the modulation of Ca(v)3.2 by the mutant ΔKelch. Our results show that the recovery phase from hyperpolarization phase determines the conformational changes that allow the α(1H) subunit to properly interact with mutant KLHL1 lacking its actin-binding Kelch domains, leading to increased Ca influx.","PeriodicalId":89176,"journal":{"name":"Journal of signal transduction","volume":"2012 ","pages":"505346"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/505346","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30800816","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

The phosphorylation-dependent regulation of mitochondrial proteins in stress responses. 线粒体蛋白在应激反应中的磷酸化依赖性调节。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2012-07-15 DOI: 10.1155/2012/931215

Yusuke Kanamaru, Shiori Sekine, Hidenori Ichijo, Kohsuke Takeda

{"title":"The phosphorylation-dependent regulation of mitochondrial proteins in stress responses.","authors":"Yusuke Kanamaru, Shiori Sekine, Hidenori Ichijo, Kohsuke Takeda","doi":"10.1155/2012/931215","DOIUrl":"https://doi.org/10.1155/2012/931215","url":null,"abstract":"To maintain cellular homeostasis, cells are equipped with precise systems that trigger the appropriate stress responses. Mitochondria not only provide cellular energy but also integrate stress response signaling pathways, including those regulating cell death. Several lines of evidence suggest that the mitochondrial proteins that function in this process, such as Bcl-2 family proteins in apoptosis and phosphoglycerate mutase family member 5 (PGAM5) in necroptosis, are regulated by several kinases. It has also been suggested that the phosphorylation-dependent regulation of mitochondrial fission machinery, dynamin-related protein 1 (Drp1), facilitates appropriate cellular stress responses. However, mitochondria themselves are also damaged by various stresses. To avoid the deleterious effects exerted by damaged mitochondria, cells remove these mitochondria in a selective autophagic degradation process called mitophagy. Interestingly, several kinases, such as PTEN-induced putative kinase 1 (PINK1) in mammals and stress-responsive mitogen-activated protein (MAP) kinases in yeast, have recently been shown to be involved in mitophagy. In this paper, we focus on the phosphorylation-dependent regulation of mitochondrial proteins and discuss the roles of this regulation in the mitochondrial and cellular stress responses.","PeriodicalId":89176,"journal":{"name":"Journal of signal transduction","volume":"2012 ","pages":"931215"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/931215","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30800818","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 53

DNA methylation, histone modifications, and signal transduction pathways: a close relationship in malignant gliomas pathophysiology. DNA甲基化、组蛋白修饰和信号转导通路:在恶性胶质瘤病理生理中的密切关系。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2012-07-17 DOI: 10.1155/2012/956958

Raúl Alelú-Paz, Nadia Ashour, Ana González-Corpas, Santiago Ropero

引用次数: 30